P54683 · TAGB_DICDI
- ProteinSerine protease/ABC transporter B family protein tagB
- GenetagB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1906 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Intercellular communication via tagB may mediate integration of cellular differentiation with morphogenesis.
Features
Showing features for active site, binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | ABC-type transporter activity | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATPase-coupled transmembrane transporter activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | proteolysis | |
Biological Process | signal transduction | |
Biological Process | sorocarp development | |
Biological Process | sorocarp stalk cell differentiation | |
Biological Process | transmembrane transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSerine protease/ABC transporter B family protein tagB
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Amoebozoa > Evosea > Eumycetozoa > Dictyostelia > Dictyosteliales > Dictyosteliaceae > Dictyostelium
Accessions
- Primary accessionP54683
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1011-1031 | Helical | ||||
Sequence: YIIIIVAGGTMVLIILLLMWI | ||||||
Transmembrane | 1076-1096 | Helical | ||||
Sequence: FIIELTIATACSLVATAASIL | ||||||
Transmembrane | 1121-1141 | Helical | ||||
Sequence: FIIIFILAFIEFLFTNVGSWI | ||||||
Transmembrane | 1210-1230 | Helical | ||||
Sequence: LVFIFTISWKLSLAFFAAVPI | ||||||
Transmembrane | 1309-1329 | Helical | ||||
Sequence: WLLIESLTFVILYFSAYLVIQ | ||||||
Transmembrane | 1332-1352 | Helical | ||||
Sequence: FTVGLMISFSLYIGYVVDASS |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Null mutations in either tagB or tagC lead to a cell autonomous defect in prestalk differentiation and a 5-fold reduction in the expression of the prestalk gene ecmA. Disruption of regA in a tagB null or in a tagC null background results in higher levels of sporulation.
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-31 | |||||
Sequence: MKFQFSSPSKIFLFSSVILILIFIGIKFELL | ||||||
Chain | PRO_0000027191 | 32-1906 | Serine protease/ABC transporter B family protein tagB | |||
Sequence: EDTNSNRNDKFNNIINRFINYNIDDSIYKNKQQQQQFSNKIYSNEKKILLKNKIIDTTIKPSININNNNNNNNKLNNNNNNNNNNNNNNNNNNNNNNNNNNNNYYNSIEYYSSFVSRLLKSNDDDGIYYDDYQSKYKKNHYIVQFKDRINDETREQLKEFLIGTDITILKEQPFKSHIVHYIPHDSFLVFMTKEQSVLLSSKEWISWIGEHEPSNKIHLNYHEKSIGYPVYIILSGSTNSLIQRWENTLNSILTSYNSKVKLTLINQKKLKSIVYCNDESPSSSSSSSCSLIGSEKIVYKWISEQSESNYIERSEKLQTANRLSPTVIFGTKDKLVNNDRIDIPLRGKGQILSIADTGLDGSHCFFSDSKYPIPFNQVNENHRKVVTYITYHDNEDYVNGHGTHVCGSAAGTPEDSSWAISSFSGLATDAKIAFYDLSSGSSEPTPPEDYSQMYKPLYDAGARVHGDSWGSVSLQGYYGGYSDDAGGIDAFLYEYPEFSILRAAGNNELFASLLAQATAKNAITVGAEQTAHVNYVSDALEYYDFSDNANFQRPCLFDKKYCNYTTAKCCSEVSNVKGLQLCCPASIKQNASDSFTTQPQFYNENNMGSFSSKGPTHDGRLKPDIVAPGEYITSARSNGENSTDQCGDGSLPNANGLMSISGTSMATPLATAATTILRQYLVDGYFPTGESVEENKLLPTGSLLKALMINNAQLLNGTYFWSASSTNPSNAIFEQINGANLIQGWGALRMNNWLYVKSSNPTPPSRWIGIGGLGKNQKATEWKEDSLSSGLNKSYCFTYKPSSSSSGSGGGGGTPRIVATLVWTDPPSYSGAKFNLVNNLDLLLLNSDDDSIITIGNSGGSLQPAGKVAQPDTLNNVEGIIINPTKAMNYKFTIAGTNVPIGPQKFSFVFHGENGQFDWADSCPQCVDGVQFPCLITNGIGIQSCGSDLLWTKCIVQSCNEGYNYNSLKNTCDKFLSYNYIIIIVAGGTMVLIILLLMWIKYQEYKESKRDSFRRFDDGTGIFVRPKDKDAKVTPPDLYNLVSPFIIELTIATACSLVATAASILQPFYIGNIVNNIPTTKSIGEFKSDFIIIFILAFIEFLFTNVGSWISGIVNEKMVMRLQNKVFRALIAQDMGFFQRNNSALLMNVLIVDTPMLRSALTGILLSIATGVCKLVGSLVFIFTISWKLSLAFFAAVPILGLVTQIQSQFTKRLTRQLLFHNSKASQHGTESLTNMHVVTNYCKQEKEMVKYSDQLMNVFITARKLIITNTFAGTGKWLLIESLTFVILYFSAYLVIQKQFTVGLMISFSLYIGYVVDASSSLFGVYVSYIQCLASATRVFMILRSAPRKRTTLEEEEADRLAGLSGGGGGGGDNGDDKKDKQNIENGKDVLPSNIITPIDNVENSNGKQDDPNNNNNNIGNLDYSEQLDGVSTVADSTVGLTKRELKKQKEKEQKEYFKQTGISVAETPTFLPSSYTELTECRGEIEFKNVSFRYPTRPDVQVLHNINMKFEAGKCYGLVGPSGSGKSTTLELISKFYPLHGETGGKIYMDGIDIAKIRPNNLRSFVTNVHQHPFLFDATIGENIGYAIDNPTQEDIIEAAKLAYAHEFINDLPKKYDTQIGEAGNLSGGQKKRIAVARAICAKRKIMLLDEITAELDPESEEAITQSIKVLTQGHTVVMVAHKVAAVRDCDKIFVLEKGYLVEEGTHDELMANKGKYYRMFSEDKDDTPLQNNNNNKNNNNNNNNNEPSSSSTPPNDQPTPPPQEQQEQKNDQPPPPPPQEQQEQQEQQQQQQQEQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQNDQPPNDYDQVPPPPPLPSESPSPPTGNNDGQPLVQMDEENDEER | ||||||
Glycosylation | 594 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 621 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 672 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 747 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 823 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1172 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1522 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1658 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 96-134 | Disordered | ||||
Sequence: INNNNNNNNKLNNNNNNNNNNNNNNNNNNNNNNNNNNNN | ||||||
Domain | 356-763 | Peptidase S8 | ||||
Sequence: PTVIFGTKDKLVNNDRIDIPLRGKGQILSIADTGLDGSHCFFSDSKYPIPFNQVNENHRKVVTYITYHDNEDYVNGHGTHVCGSAAGTPEDSSWAISSFSGLATDAKIAFYDLSSGSSEPTPPEDYSQMYKPLYDAGARVHGDSWGSVSLQGYYGGYSDDAGGIDAFLYEYPEFSILRAAGNNELFASLLAQATAKNAITVGAEQTAHVNYVSDALEYYDFSDNANFQRPCLFDKKYCNYTTAKCCSEVSNVKGLQLCCPASIKQNASDSFTTQPQFYNENNMGSFSSKGPTHDGRLKPDIVAPGEYITSARSNGENSTDQCGDGSLPNANGLMSISGTSMATPLATAATTILRQYLVDGYFPTGESVEENKLLPTGSLLKALMINNAQLLNGTYFWSASSTNPSNAI | ||||||
Domain | 1080-1363 | ABC transmembrane type-1 | ||||
Sequence: LTIATACSLVATAASILQPFYIGNIVNNIPTTKSIGEFKSDFIIIFILAFIEFLFTNVGSWISGIVNEKMVMRLQNKVFRALIAQDMGFFQRNNSALLMNVLIVDTPMLRSALTGILLSIATGVCKLVGSLVFIFTISWKLSLAFFAAVPILGLVTQIQSQFTKRLTRQLLFHNSKASQHGTESLTNMHVVTNYCKQEKEMVKYSDQLMNVFITARKLIITNTFAGTGKWLLIESLTFVILYFSAYLVIQKQFTVGLMISFSLYIGYVVDASSSLFGVYVSYIQ | ||||||
Region | 1385-1455 | Disordered | ||||
Sequence: LEEEEADRLAGLSGGGGGGGDNGDDKKDKQNIENGKDVLPSNIITPIDNVENSNGKQDDPNNNNNNIGNLD | ||||||
Compositional bias | 1429-1455 | Polar residues | ||||
Sequence: TPIDNVENSNGKQDDPNNNNNNIGNLD | ||||||
Domain | 1518-1756 | ABC transporter | ||||
Sequence: IEFKNVSFRYPTRPDVQVLHNINMKFEAGKCYGLVGPSGSGKSTTLELISKFYPLHGETGGKIYMDGIDIAKIRPNNLRSFVTNVHQHPFLFDATIGENIGYAIDNPTQEDIIEAAKLAYAHEFINDLPKKYDTQIGEAGNLSGGQKKRIAVARAICAKRKIMLLDEITAELDPESEEAITQSIKVLTQGHTVVMVAHKVAAVRDCDKIFVLEKGYLVEEGTHDELMANKGKYYRMFSE | ||||||
Region | 1757-1906 | Disordered | ||||
Sequence: DKDDTPLQNNNNNKNNNNNNNNNEPSSSSTPPNDQPTPPPQEQQEQKNDQPPPPPPQEQQEQQEQQQQQQQEQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQNDQPPNDYDQVPPPPPLPSESPSPPTGNNDGQPLVQMDEENDEER | ||||||
Compositional bias | 1760-1786 | Polar residues | ||||
Sequence: DTPLQNNNNNKNNNNNNNNNEPSSSST | ||||||
Compositional bias | 1787-1815 | Pro residues | ||||
Sequence: PPNDQPTPPPQEQQEQKNDQPPPPPPQEQ | ||||||
Compositional bias | 1816-1867 | Polar residues | ||||
Sequence: QEQQEQQQQQQQEQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQNDQPPN | ||||||
Compositional bias | 1868-1884 | Pro residues | ||||
Sequence: DYDQVPPPPPLPSESPS |
Sequence similarities
In the C-terminal section; belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
In the N-terminal section; belongs to the peptidase S8 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,906
- Mass (Da)212,647
- Last updated2007-12-04 v2
- ChecksumCCAAD3D6857CED20
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1429-1455 | Polar residues | ||||
Sequence: TPIDNVENSNGKQDDPNNNNNNIGNLD | ||||||
Compositional bias | 1760-1786 | Polar residues | ||||
Sequence: DTPLQNNNNNKNNNNNNNNNEPSSSST | ||||||
Compositional bias | 1787-1815 | Pro residues | ||||
Sequence: PPNDQPTPPPQEQQEQKNDQPPPPPPQEQ | ||||||
Compositional bias | 1816-1867 | Polar residues | ||||
Sequence: QEQQEQQQQQQQEQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQNDQPPN | ||||||
Sequence conflict | 1829 | in Ref. 1; AAA62212 | ||||
Sequence: Missing | ||||||
Compositional bias | 1868-1884 | Pro residues | ||||
Sequence: DYDQVPPPPPLPSESPS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U20432 EMBL· GenBank· DDBJ | AAA62212.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAFI02000085 EMBL· GenBank· DDBJ | EAL64352.1 EMBL· GenBank· DDBJ | Genomic DNA |