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Entry version 111 (13 Nov 2019)
Sequence version 1 (20 Dec 2005)
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Protein

Bifunctional glutathionylspermidine synthetase/amidase

Gene

gss

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. In vitro, the amidase active site also catalyzes hydrolysis of amide and ester derivatives of glutathione (e.g. glutathione ethyl ester and glutathione amide) but lacks activity toward acetylspermidine (N1 and N8) and acetylspermine (N1).4 Publications

Miscellaneous

Gsp forms mixed disulfides with the thiols of a variety of E.coli proteins. These mixed disulfides represent a previously uncharacterized type of post-translational modification. The level of these proteins is increased by oxidative stress, which implies that Gsp might protect protein thiols against irreversible oxidation (PubMed:20530482).1 Publication
No metal ion is required for the amidase activity.1 Publication
Gsp hydrolysis to GSH and spermidine proceeds with formation of a glutathionyl acyl-enzyme intermediate, utilizing a cysteine residue as the catalytic nucleophile (PubMed:9398217). For Gsp synthesis, GSH is likely phosphorylated at one of two GSH-binding sites to form an acylphosphate intermediate that then translocates to the other site for subsequent nucleophilic addition of spermidine (PubMed:17124497).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

When exposed to oxidative stress, Gsp amidase activity is transiently inhibited in vivo by oxidation of the catalytic Cys-59 thiol to sulfenic acid; this modification does not affect Gsp synthetase activity. Gsp amidase activity is negatively autoregulated by the Gsp synthetase domain, and is activated by the Gsp synthetase substrates, GSH and ATP-Mg2+; the occupancy of the synthetase active site may initiate communication through the protein as manifest by the release of inhibition of the amidase activity. A tetrahedral phosphonate analog of glutathionylspermidine, designed as a mimic of the proposed tetrahedral intermediate for either reaction, inhibits the synthetase activity (Ki of 10 µM) but does not inhibit the amidase activity. Amidase activity is inhibited by iodoacetamide in vitro.3 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 7 sec(-1) for Gsp synthetase activity at pH 6.8 and 2.1 sec(-1) for Gsp amidase activity at pH 7.5.1 Publication
  1. KM=100 µM for ATP (at pH 6.8)2 Publications
  2. KM=800 µM for glutathione (at pH 6.8)2 Publications
  3. KM=218 µM for glutathione2 Publications
  4. KM=60 µM for spermidine (at pH 6.8)2 Publications
  5. KM=20 µM for spermidine (at pH 7.5)2 Publications
  6. KM=76 µM for spermidine2 Publications
  7. KM=900 µM for glutathionylspermidine (at pH 7.5)2 Publications

    pH dependencei

    Optimum pH is around 6.8 for Gsp synthetase activity.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glutathione metabolism

    This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.
    View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.

    Pathwayi: spermidine metabolism

    This protein is involved in the pathway spermidine metabolism, which is part of Amine and polyamine metabolism.
    View all proteins of this organism that are known to be involved in the pathway spermidine metabolism and in Amine and polyamine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei58Gsp1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei59S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine intermediate1 Publication1
    Binding sitei64Gsp1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei131Increases nucleophilicity of active site Cys; for amidase activity1
    Binding sitei149Gsp1
    Binding sitei316Glutathione1
    Sitei316Transition state stabilizer; for synthetase activity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi318Magnesium 11
    Metal bindingi330Magnesium 11
    Metal bindingi330Magnesium 21
    Metal bindingi332Magnesium 21
    Binding sitei335Glutathione1
    Binding sitei391Spermidine1
    Binding sitei392Glutathione1
    Binding sitei446Glutathione1
    Binding sitei498ATP1
    Binding sitei533ATP1
    Binding sitei582ATP1
    Binding sitei610Spermidine1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi316 – 318ATP3
    Nucleotide bindingi539 – 540ATP2
    Nucleotide bindingi568 – 571ATP4
    Nucleotide bindingi603 – 605ATP3

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase, Ligase, Multifunctional enzyme
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:GSP-MONOMER
    ECOL316407:JW2956-MONOMER
    MetaCyc:GSP-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.5.1.78 2026
    6.3.1.8 2026

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00204
    UPA00819

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    C51.A01

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Bifunctional glutathionylspermidine synthetase/amidase
    Short name:
    GspSA
    Including the following 2 domains:
    Glutathionylspermidine amidase (EC:3.5.1.784 Publications)
    Short name:
    Gsp amidase
    Alternative name(s):
    Glutathionylspermidine amidohydrolase [spermidine-forming]
    Glutathionylspermidine synthetase (EC:6.3.1.84 Publications)
    Short name:
    Gsp synthetase
    Alternative name(s):
    Glutathione:spermidine ligase [ADP-forming]
    Gsp synthase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:gss
    Synonyms:gsp
    Ordered Locus Names:b2988, JW2956
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene do not produce Gsp under anaerobic conditions. Cells lacking both this gene and glutaredoxin (grxA or grxB) become hypersensitive to H2O2; they are even more susceptible to oxidative damage than the single mutant lacking glutaredoxin only.2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi59C → A: Loss of amidase activity. 1 Publication1
    Mutagenesisi173C → A: No effect on amidase activity. 1 Publication1
    Mutagenesisi316R → E: Loss of synthetase activity. 1
    Mutagenesisi335S → A: 3.6-fold decrease in GSH affinity, 1.6-fold decrease in spermidine activity, and 1.3-fold decrease in synthetase activity. 1 Publication1
    Mutagenesisi337S → A: No effect on GSH and spermidine affinity, but 2-fold decrease in synthetase activity. 1 Publication1
    Mutagenesisi338C → A: 10-fold decrease in GSH affinity, 5-fold decrease in spermidine activity, but no effect on synthetase activity. 1 Publication1
    Mutagenesisi391E → A: 2-fold decrease in GSH affinity, 60-fold decrease in spermidine activity, and 10-fold decrease in synthetase activity. 1 Publication1
    Mutagenesisi392E → A: 33-fold decrease in GSH affinity, 13-fold decrease in spermidine activity, and 6-fold decrease in synthetase activity. 1 Publication1
    Mutagenesisi441T → A: 3-fold decrease in GSH affinity, 21-fold decrease in spermidine activity, and 17-fold decrease in synthetase activity. 1 Publication1
    Mutagenesisi538R → A: 6-fold decrease in GSH affinity, 2.4-fold decrease in spermidine activity, and 4-fold decrease in synthetase activity. 1 Publication1
    Mutagenesisi598R → A: 10-fold increase in GSH affinity, 9-fold decrease in spermidine activity, and 15-fold decrease in synthetase activity. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000704432 – 619Bifunctional glutathionylspermidine synthetase/amidaseAdd BLAST618

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei59Cysteine sulfenic acid (-SOH); transient1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Oxidation of Cys-59 to sulfenic acid during oxidative stress selectively inhibits the amidase activity which leads to a rapid increase in the amounts of intracellular Gsp and Gsp S-thiolated proteins (GspSSPs).1 Publication

    Keywords - PTMi

    Oxidation

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0AES0

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P0AES0

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0AES0

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Expression level is unaffected by H2O2; however Gsp rapidly accumulates in E.coli in the presence of H2O2.

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4261180, 18 interactors
    851792, 4 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-36018N

    Protein interaction database and analysis system

    More...
    IntActi
    P0AES0, 14 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2988

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1619
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P0AES0

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0AES0

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini34 – 176Peptidase C51PROSITE-ProRule annotationAdd BLAST143

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 195Gsp amidaseAdd BLAST194
    Regioni78 – 81Gsp binding4
    Regioni196 – 205Linker10
    Regioni206 – 619Gsp synthetaseAdd BLAST414

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The two activities reside in distinct domains (N-terminal amidase and C-terminal synthetase). The two domains expressed independently are folded and functional; liberation of the amidase domain from the synthetase domain highly activates the amidase activity.2 Publications

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4106032 Bacteria
    COG0754 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000124980

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0AES0

    KEGG Orthology (KO)

    More...
    KOi
    K01460

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR007921 CHAP_dom
    IPR005494 GSPS_pre-ATP-grasp-like_dom
    IPR038765 Papain-like_cys_pep_sf
    IPR016185 PreATP-grasp_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF05257 CHAP, 1 hit
    PF03738 GSP_synth, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52440 SSF52440, 1 hit
    SSF54001 SSF54001, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50911 CHAP, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AES0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSKGTTSQDA PFGTLLGYAP GGVAIYSSDY SSLDPQEYED DAVFRSYIDD
    60 70 80 90 100
    EYMGHKWQCV EFARRFLFLN YGVVFTDVGM AWEIFSLRFL REVVNDNILP
    110 120 130 140 150
    LQAFPNGSPR APVAGALLIW DKGGEFKDTG HVAIITQLHG NKVRIAEQNV
    160 170 180 190 200
    IHSPLPQGQQ WTRELEMVVE NGCYTLKDTF DDTTILGWMI QTEDTEYSLP
    210 220 230 240 250
    QPEIAGELLK ISGARLENKG QFDGKWLDEK DPLQNAYVQA NGQVINQDPY
    260 270 280 290 300
    HYYTITESAE QELIKATNEL HLMYLHATDK VLKDDNLLAL FDIPKILWPR
    310 320 330 340 350
    LRLSWQRRRH HMITGRMDFC MDERGLKVYE YNADSASCHT EAGLILERWA
    360 370 380 390 400
    EQGYKGNGFN PAEGLINELA GAWKHSRARP FVHIMQDKDI EENYHAQFME
    410 420 430 440 450
    QALHQAGFET RILRGLDELG WDAAGQLIDG EGRLVNCVWK TWAWETAFDQ
    460 470 480 490 500
    IREVSDREFA AVPIRTGHPQ NEVRLIDVLL RPEVLVFEPL WTVIPGNKAI
    510 520 530 540 550
    LPILWSLFPH HRYLLDTDFT VNDELVKTGY AVKPIAGRCG SNIDLVSHHE
    560 570 580 590 600
    EVLDKTSGKF AEQKNIYQQL WCLPKVDGKY IQVCTFTVGG NYGGTCLRGD
    610
    ESLVIKKESD IEPLIVVKK
    Length:619
    Mass (Da):70,532
    Last modified:December 20, 2005 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i07FB43D8A0B2933C
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    U23148 Genomic DNA Translation: AAC43339.1
    U28377 Genomic DNA Translation: AAA69155.1
    U00096 Genomic DNA Translation: AAC76024.1
    AP009048 Genomic DNA Translation: BAE77049.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A57538

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417462.1, NC_000913.3
    WP_001297309.1, NZ_SSZK01000023.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76024; AAC76024; b2988
    BAE77049; BAE77049; BAE77049

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947474

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2956
    eco:b2988

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.3741

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U23148 Genomic DNA Translation: AAC43339.1
    U28377 Genomic DNA Translation: AAA69155.1
    U00096 Genomic DNA Translation: AAC76024.1
    AP009048 Genomic DNA Translation: BAE77049.1
    PIRiA57538
    RefSeqiNP_417462.1, NC_000913.3
    WP_001297309.1, NZ_SSZK01000023.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2IO7X-ray2.70A/B1-619[»]
    2IO8X-ray2.10A/B1-619[»]
    2IO9X-ray2.20A/B1-619[»]
    2IOAX-ray2.80A/B1-619[»]
    2IOBX-ray2.20A/B1-619[»]
    3A2YX-ray1.95A1-197[»]
    3A2ZX-ray1.50A1-197[»]
    3A30X-ray2.20A1-197[»]
    3O98X-ray2.80A/B1-619[»]
    SMRiP0AES0
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4261180, 18 interactors
    851792, 4 interactors
    DIPiDIP-36018N
    IntActiP0AES0, 14 interactors
    STRINGi511145.b2988

    Protein family/group databases

    MEROPSiC51.A01

    Proteomic databases

    jPOSTiP0AES0
    PaxDbiP0AES0
    PRIDEiP0AES0

    Genome annotation databases

    EnsemblBacteriaiAAC76024; AAC76024; b2988
    BAE77049; BAE77049; BAE77049
    GeneIDi947474
    KEGGiecj:JW2956
    eco:b2988
    PATRICifig|1411691.4.peg.3741

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB2720

    Phylogenomic databases

    eggNOGiENOG4106032 Bacteria
    COG0754 LUCA
    HOGENOMiHOG000124980
    InParanoidiP0AES0
    KOiK01460

    Enzyme and pathway databases

    UniPathwayiUPA00204
    UPA00819
    BioCyciEcoCyc:GSP-MONOMER
    ECOL316407:JW2956-MONOMER
    MetaCyc:GSP-MONOMER
    BRENDAi3.5.1.78 2026
    6.3.1.8 2026

    Miscellaneous databases

    EvolutionaryTraceiP0AES0

    Protein Ontology

    More...
    PROi
    PR:P0AES0

    Family and domain databases

    InterProiView protein in InterPro
    IPR007921 CHAP_dom
    IPR005494 GSPS_pre-ATP-grasp-like_dom
    IPR038765 Papain-like_cys_pep_sf
    IPR016185 PreATP-grasp_dom_sf
    PfamiView protein in Pfam
    PF05257 CHAP, 1 hit
    PF03738 GSP_synth, 1 hit
    SUPFAMiSSF52440 SSF52440, 1 hit
    SSF54001 SSF54001, 1 hit
    PROSITEiView protein in PROSITE
    PS50911 CHAP, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGSP_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AES0
    Secondary accession number(s): P43675, Q2M9K7
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: November 13, 2019
    This is version 111 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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