P15028 · FECB_ECOLI
- ProteinFe(3+) dicitrate-binding periplasmic protein FecB
- GenefecB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids300 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Part of the ABC transporter complex FecBCDE involved in citrate-dependent Fe3+ uptake (PubMed:17660286, PubMed:2651410).
Binds both iron-free and iron-loaded citrate although it binds iron-loaded citrate with a higher affinity (PubMed:26600288).
Binds different forms of Fe3+-citrate as well as citrate complexed with various representative Fe3+-mimics (Ga3+, Al3+, Sc3+ and In3+) and a representative divalent metal ion (Mg2+) (PubMed:26600288).
Can also bind various tricarboxylates in iron-free and iron-loaded form (PubMed:26600288).
Binds both iron-free and iron-loaded citrate although it binds iron-loaded citrate with a higher affinity (PubMed:26600288).
Binds different forms of Fe3+-citrate as well as citrate complexed with various representative Fe3+-mimics (Ga3+, Al3+, Sc3+ and In3+) and a representative divalent metal ion (Mg2+) (PubMed:26600288).
Can also bind various tricarboxylates in iron-free and iron-loaded form (PubMed:26600288).
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 | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing | |
Cellular Component | membrane | |
Cellular Component | outer membrane-bounded periplasmic space | |
Biological Process | intracellular iron ion homeostasis | |
Biological Process | iron import into cell | |
Biological Process | response to iron ion | |
Biological Process | siderophore-dependent iron import into cell |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameFe(3+) dicitrate-binding periplasmic protein FecB
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP15028
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 8 | in strain: B | ||||
Sequence: L → V | ||||||
Mutagenesis | 68 | No change in citrate-mediated Fe3+ transport. | ||||
Sequence: K → C | ||||||
Mutagenesis | 69 | NO change in citrate-mediated Fe3+ transport. | ||||
Sequence: R → C | ||||||
Mutagenesis | 93 | Retains 10% of wild-type citrate-mediated Fe3+ transport. | ||||
Sequence: E → A | ||||||
Mutagenesis | 93 | Retains 17% of wild-type citrate-mediated Fe3+ transport. | ||||
Sequence: E → C | ||||||
Mutagenesis | 93 | Retains 13% of wild-type citrate-mediated Fe3+ transport. | ||||
Sequence: E → R | ||||||
Mutagenesis | 183 | Retains 13% of wild-type citrate-mediated Fe3+ transport. | ||||
Sequence: R → C | ||||||
Mutagenesis | 222 | Retains 26% of wild-type citrate-mediated Fe3+ transport. | ||||
Sequence: E → A | ||||||
Mutagenesis | 222 | Retains 32% of wild-type citrate-mediated Fe3+ transport. | ||||
Sequence: E → C | ||||||
Mutagenesis | 222 | Retains 16% of wild-type citrate-mediated Fe3+ transport. | ||||
Sequence: E → R | ||||||
Mutagenesis | 245 | Retains 95% of wild-type citrate-mediated Fe3+ transport. | ||||
Sequence: R → C | ||||||
Mutagenesis | 246 | Retains 8% of wild-type citrate-mediated Fe3+ transport. | ||||
Sequence: W → C | ||||||
Mutagenesis | 248 | Retains 92% of wild-type citrate-mediated Fe3+ transport. | ||||
Sequence: Q → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
Miscellaneous
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MLAFIRFLFAGLLLVISHAFA | ||||||
Chain | PRO_0000031820 | 22-300 | Fe3+ dicitrate-binding periplasmic protein FecB | |||
Sequence: ATVQDEHGTFTLEKTPQRIVVLELSFADALAAVDVIPIGIADDNDAKRILPEVRAHLKPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVYIALQQIAPVLLLKSRNETYAENLQSAAIIGEMVGKKREMQARLEQHKERMAQWASQLPKGTRVAFGTSREQQFNLHTQETWTGSVLASLGLNVPAAMAGASMPSIGLEQLLAVNPAWLLVAHYREESIVKRWQQDPLWQMLTAAQKQQVASVDSNTWARMRGIFAAERIAADTVKIFHHQPLTVVK |
Proteomic databases
Expression
Induction
Induced 1.8-fold by hydroxyurea.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-295 | Fe/B12 periplasmic-binding | ||||
Sequence: RIVVLELSFADALAAVDVIPIGIADDNDAKRILPEVRAHLKPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVYIALQQIAPVLLLKSRNETYAENLQSAAIIGEMVGKKREMQARLEQHKERMAQWASQLPKGTRVAFGTSREQQFNLHTQETWTGSVLASLGLNVPAAMAGASMPSIGLEQLLAVNPAWLLVAHYREESIVKRWQQDPLWQMLTAAQKQQVASVDSNTWARMRGIFAAERIAADTVKIFHHQP |
Sequence similarities
Belongs to the bacterial solute-binding protein 8 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length300
- Mass (Da)33,146
- Last updated2003-07-19 v3
- Checksum6024ED0F9C82D0EA
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 23 | in Ref. 1; AAA23762 | ||||
Sequence: T → M | ||||||
Sequence conflict | 57 | in Ref. 1; AAA23762 | ||||
Sequence: I → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M26397 EMBL· GenBank· DDBJ | AAA23762.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U14003 EMBL· GenBank· DDBJ | AAA97186.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U00096 EMBL· GenBank· DDBJ | AAC77246.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE78281.1 EMBL· GenBank· DDBJ | Genomic DNA |