O07576 · BCAP_BACSU
- ProteinBranched-chain amino acid permease BcaP
- GenebcaP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids465 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Branched-chain amino acid transport system which is involved in the uptake of isoleucine, valine and probably leucine (PubMed:25645558).
Can also transport threonine, and is active as a minor serine permease (PubMed:25645558, PubMed:32743959).
May be an amino acid permease of rather broad specificity, because several amino acids, albeit at 100-fold excess, are able to prevent isoleucine uptake (PubMed:25645558).
Probably does not transport methionine (PubMed:25645558).
Together with BraB and BrnQ, plays an important role in the activation of CodY, a branched-chain amino acid-responsive transcriptional regulator that controls the expression of several dozen transcription units in B.subtilis (PubMed:25645558).
Can also transport threonine, and is active as a minor serine permease (PubMed:25645558, PubMed:32743959).
May be an amino acid permease of rather broad specificity, because several amino acids, albeit at 100-fold excess, are able to prevent isoleucine uptake (PubMed:25645558).
Probably does not transport methionine (PubMed:25645558).
Together with BraB and BrnQ, plays an important role in the activation of CodY, a branched-chain amino acid-responsive transcriptional regulator that controls the expression of several dozen transcription units in B.subtilis (PubMed:25645558).
Activity regulation
Isoleucine uptake is efficiently reduced in the presence of 100-fold excess valine, leucine, alanine, threonine, serine, cysteine, asparagine, and a nonproteinaceous amino acid 4-azaleucine.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
4.1 μM | isoleucine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
15 nmol/min/mg | with isoleucine as substrate |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | amino acid transmembrane transporter activity | |
Biological Process | amino acid transport |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBranched-chain amino acid permease BcaP
- Short namesBCAA permease
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionO07576
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 35-55 | Helical | ||||
Sequence: LLGIGAIIGTGIFVLTGTGAV | ||||||
Transmembrane | 57-77 | Helical | ||||
Sequence: AGPGLTISFVVAALACLFAAL | ||||||
Transmembrane | 103-123 | Helical | ||||
Sequence: LMAFIIGWDLILEYMLAVSAV | ||||||
Transmembrane | 133-153 | Helical | ||||
Sequence: SFLSGLGIHLPVALTAAPGAV | ||||||
Transmembrane | 159-179 | Helical | ||||
Sequence: LFNLPAFVIVMAITYLLYLGI | ||||||
Transmembrane | 188-208 | Helical | ||||
Sequence: IMVILKILVVLLFIAVAAVYV | ||||||
Transmembrane | 216-236 | Helical | ||||
Sequence: FMPMGFGGVFSAAALVFFAFI | ||||||
Transmembrane | 258-278 | Helical | ||||
Sequence: GIIFSLLVCTILYVTVSAIMT | ||||||
Transmembrane | 305-325 | Helical | ||||
Sequence: VAGIIDIGAVLGMTTVMLVML | ||||||
Transmembrane | 355-375 | Helical | ||||
Sequence: PYVATWFFGTMSALLGSLVPL | ||||||
Transmembrane | 380-400 | Helical | ||||
Sequence: KLVNIGTLSAFVLISVAVIVL | ||||||
Transmembrane | 413-432 | Helical | ||||
Sequence: CPGVPVIPGLAILFCLFLIL | ||||||
Transmembrane | 437-456 | Helical | ||||
Sequence: VTIVRFLVWLLIGLVIYFLY |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mutant is still able to take up isoleucine, leucine and valine (PubMed:25645558).
Deletion of the gene confers a weak resistance to growth inhibition by serine (PubMed:32743959).
The deletion of the three permease-encoding genes aimA (ybeC), ybxG and bcaP results in an unprecedented resistance to serine up to 100 mM (PubMed:32743959).
Deletion of the gene confers a weak resistance to growth inhibition by serine (PubMed:32743959).
The deletion of the three permease-encoding genes aimA (ybeC), ybxG and bcaP results in an unprecedented resistance to serine up to 100 mM (PubMed:32743959).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000360836 | 1-465 | Branched-chain amino acid permease BcaP | |||
Sequence: MKGSVFRKKSIQDLIAATSGEKSLKRELGAFDLTLLGIGAIIGTGIFVLTGTGAVTAGPGLTISFVVAALACLFAALSYAEFASSVPVSGSVYTFTYATLGELMAFIIGWDLILEYMLAVSAVSVGWSGYFQSFLSGLGIHLPVALTAAPGAVKGTFTLFNLPAFVIVMAITYLLYLGIKESKRVNNIMVILKILVVLLFIAVAAVYVKPHNWQPFMPMGFGGVFSAAALVFFAFIGFDAVSSAAEETKNPAKDLPKGIIFSLLVCTILYVTVSAIMTGVIPFAQFAGVDHPVSLVLQSAGQNWVAGIIDIGAVLGMTTVMLVMLYGQTRVMFAMSRDGLVPGSLSKVHPKHKTPYVATWFFGTMSALLGSLVPLDELAKLVNIGTLSAFVLISVAVIVLRKKQPDLPRAFKCPGVPVIPGLAILFCLFLILNLGWVTIVRFLVWLLIGLVIYFLYSRKHSKLNQ |
Proteomic databases
Expression
Induction
Expression is repressed by the transcriptional regulator CodY (PubMed:12618455, PubMed:21097623).
Contains two CodY-binding sites in the bcaP regulatory region, which both contribute to repression in vivo and do so independently of each other (PubMed:21097623).
A single CodY-binding site is apparently sufficient for substantial CodY-dependent regulation, but both upstream and downstram CodY-binding regions are required for maximal repression of bcaP (PubMed:21097623).
Efficient bcaP repression by CodY requires the simultaneous presence of isoleucine, leucine and valine, and other amino acids in the growth medium (PubMed:21097623).
Contains two CodY-binding sites in the bcaP regulatory region, which both contribute to repression in vivo and do so independently of each other (PubMed:21097623).
A single CodY-binding site is apparently sufficient for substantial CodY-dependent regulation, but both upstream and downstram CodY-binding regions are required for maximal repression of bcaP (PubMed:21097623).
Efficient bcaP repression by CodY requires the simultaneous presence of isoleucine, leucine and valine, and other amino acids in the growth medium (PubMed:21097623).
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length465
- Mass (Da)49,711
- Last updated1997-07-01 v1
- ChecksumCC4A815DBA426A94
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y14082 EMBL· GenBank· DDBJ | CAA74491.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB12785.1 EMBL· GenBank· DDBJ | Genomic DNA |