UniProtKB - P06709 (BIRA_ECOLI)
Bifunctional ligase/repressor BirA
birA
Functioni
Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
UniRule annotation4 PublicationsCatalytic activityi
- ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H+ + N6-biotinyl-L-lysyl-[protein]UniRule annotation2 PublicationsEC:6.3.4.15UniRule annotation2 Publications
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 112 | BiotinUniRule annotation2 Publications | 1 | |
Binding sitei | 183 | BiotinUniRule annotation2 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 22 – 41 | H-T-H motifUniRule annotationAdd BLAST | 20 |
GO - Molecular functioni
- ATP binding Source: CAFA
- biotin-[acetyl-CoA-carboxylase] ligase activity Source: EcoliWiki
- biotin binding Source: CAFA
- DNA binding Source: EcoliWiki
- protein homodimerization activity Source: CAFA
- transcription cis-regulatory region binding Source: CAFA
GO - Biological processi
- biotin biosynthetic process Source: EcoliWiki
- biotin metabolic process Source: CAFA
- protein biotinylation Source: CACAO
- regulation of transcription, DNA-templated Source: UniProtKB-UniRule
Keywordsi
Molecular function | DNA-binding, Ligase, Repressor |
Biological process | Transcription, Transcription regulation |
Ligand | ATP-binding, Biotin, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:BIOTINLIG-MONOMER |
BRENDAi | 6.3.4.15, 2026 |
Protein family/group databases
MoonProti | P06709 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional ligase/repressor BirAUniRule annotationAlternative name(s): Biotin operon repressorUniRule annotation Biotin--[acetyl-CoA-carboxylase] ligaseUniRule annotation (EC:6.3.4.15UniRule annotation) Biotin--protein ligaseUniRule annotation Biotin-[acetyl-CoA carboxylase] synthetaseUniRule annotation |
Gene namesi | Name:birAUniRule annotation Synonyms:bioR, dhbB Ordered Locus Names:b3973, JW3941 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Other locations
- cytoplasm Source: GO_Central
- transcription repressor complex Source: CAFA
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 52 | T → I: Does not affect repressor activity. 1 Publication | 1 | |
Mutagenesisi | 52 | T → S: 5-fold increase of repressor activity. Increases binding to DNA. 1 Publication | 1 | |
Mutagenesisi | 57 | G → S: Lack of repressor activity. Does not bind DNA. 1 Publication | 1 | |
Mutagenesisi | 58 | Y → F: Lack of repressor activity. 1 Publication | 1 | |
Mutagenesisi | 58 | Y → T: Does not affect repressor activity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3559644 |
DrugBanki | DB04651, BIOTINOL-5-AMP |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000064932 | 1 – 321 | Bifunctional ligase/repressor BirAAdd BLAST | 321 |
Proteomic databases
jPOSTi | P06709 |
PaxDbi | P06709 |
PRIDEi | P06709 |
Interactioni
Subunit structurei
Monomer in solution.
Interacts with BCCP. Homodimerizes to bind DNA. Interaction with the corepressor bio-5'-AMP increases dimerization.
6 PublicationsBinary interactionsi
P06709
With | #Exp. | IntAct |
---|---|---|
nanE [P0A761] | 2 | EBI-545740,EBI-561432 |
GO - Molecular functioni
- protein homodimerization activity Source: CAFA
Protein-protein interaction databases
BioGRIDi | 4263391, 269 interactors |
DIPi | DIP-9224N |
IntActi | P06709, 7 interactors |
STRINGi | 511145.b3973 |
Chemistry databases
BindingDBi | P06709 |
Structurei
Secondary structure
3D structure databases
SMRi | P06709 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P06709 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 67 – 254 | BPL/LPL catalyticPROSITE-ProRule annotationAdd BLAST | 188 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 89 – 91 | Biotin binding | 3 | |
Regioni | 116 – 118 | Biotin binding | 3 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0340, Bacteria COG1654, Bacteria |
HOGENOMi | CLU_051096_4_0_6 |
InParanoidi | P06709 |
PhylomeDBi | P06709 |
Family and domain databases
CDDi | cd16442, BPL, 1 hit |
DisProti | DP00349 |
Gene3Di | 1.10.10.10, 1 hit 3.30.930.10, 1 hit |
HAMAPi | MF_00978, Bifunct_BirA, 1 hit |
InterProi | View protein in InterPro IPR045864, aa-tRNA-synth_II/BPL/LPL IPR030855, Bifunct_BirA IPR004408, Biotin_CoA_COase_ligase IPR004409, Biotin_operon_repress_HTH IPR003142, BPL_C IPR004143, BPL_LPL_catalytic IPR013196, HTH_11 IPR008988, Transcriptional_repressor_C IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
Pfami | View protein in Pfam PF02237, BPL_C, 1 hit PF03099, BPL_LplA_LipB, 1 hit PF08279, HTH_11, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit SSF50037, SSF50037, 1 hit SSF55681, SSF55681, 1 hit |
TIGRFAMsi | TIGR00121, birA_ligase, 1 hit TIGR00122, birA_repr_reg, 1 hit |
PROSITEi | View protein in PROSITE PS51733, BPL_LPL_CATALYTIC, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MKDNTVPLKL IALLANGEFH SGEQLGETLG MSRAAINKHI QTLRDWGVDV
60 70 80 90 100
FTVPGKGYSL PEPIQLLNAK QILGQLDGGS VAVLPVIDST NQYLLDRIGE
110 120 130 140 150
LKSGDACIAE YQQAGRGRRG RKWFSPFGAN LYLSMFWRLE QGPAAAIGLS
160 170 180 190 200
LVIGIVMAEV LRKLGADKVR VKWPNDLYLQ DRKLAGILVE LTGKTGDAAQ
210 220 230 240 250
IVIGAGINMA MRRVEESVVN QGWITLQEAG INLDRNTLAA MLIRELRAAL
260 270 280 290 300
ELFEQEGLAP YLSRWEKLDN FINRPVKLII GDKEIFGISR GIDKQGALLL
310 320
EQDGIIKPWM GGEISLRSAE K
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 61 | P → A in strain: RDD012. | 1 | |
Natural varianti | 70 | K → E in strain: RDD012. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M10123 Genomic DNA Translation: AAA23520.1 M15820 Genomic DNA Translation: AAA23521.1 L14557 Genomic DNA Translation: AAA24186.1 U00006 Genomic DNA Translation: AAC43075.1 U00096 Genomic DNA Translation: AAC76951.1 AP009048 Genomic DNA Translation: BAE77342.1 |
PIRi | B24029, BVECBF |
RefSeqi | NP_418404.1, NC_000913.3 WP_000654630.1, NZ_SSZK01000084.1 |
Genome annotation databases
EnsemblBacteriai | AAC76951; AAC76951; b3973 BAE77342; BAE77342; BAE77342 |
GeneIDi | 58463579 948469 |
KEGGi | ecj:JW3941 eco:b3973 |
PATRICi | fig|1411691.4.peg.2735 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M10123 Genomic DNA Translation: AAA23520.1 M15820 Genomic DNA Translation: AAA23521.1 L14557 Genomic DNA Translation: AAA24186.1 U00006 Genomic DNA Translation: AAC43075.1 U00096 Genomic DNA Translation: AAC76951.1 AP009048 Genomic DNA Translation: BAE77342.1 |
PIRi | B24029, BVECBF |
RefSeqi | NP_418404.1, NC_000913.3 WP_000654630.1, NZ_SSZK01000084.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BIA | X-ray | 2.30 | A | 1-321 | [»] | |
1BIB | X-ray | 2.80 | A | 1-321 | [»] | |
1HXD | X-ray | 2.40 | A/B | 1-321 | [»] | |
2EWN | X-ray | 2.80 | A/B | 1-321 | [»] | |
4WF2 | X-ray | 2.31 | A | 1-321 | [»] | |
SMRi | P06709 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263391, 269 interactors |
DIPi | DIP-9224N |
IntActi | P06709, 7 interactors |
STRINGi | 511145.b3973 |
Chemistry databases
BindingDBi | P06709 |
ChEMBLi | CHEMBL3559644 |
DrugBanki | DB04651, BIOTINOL-5-AMP |
Protein family/group databases
MoonProti | P06709 |
Proteomic databases
jPOSTi | P06709 |
PaxDbi | P06709 |
PRIDEi | P06709 |
Genome annotation databases
EnsemblBacteriai | AAC76951; AAC76951; b3973 BAE77342; BAE77342; BAE77342 |
GeneIDi | 58463579 948469 |
KEGGi | ecj:JW3941 eco:b3973 |
PATRICi | fig|1411691.4.peg.2735 |
Organism-specific databases
EchoBASEi | EB0121 |
Phylogenomic databases
eggNOGi | COG0340, Bacteria COG1654, Bacteria |
HOGENOMi | CLU_051096_4_0_6 |
InParanoidi | P06709 |
PhylomeDBi | P06709 |
Enzyme and pathway databases
BioCyci | EcoCyc:BIOTINLIG-MONOMER |
BRENDAi | 6.3.4.15, 2026 |
Miscellaneous databases
EvolutionaryTracei | P06709 |
PROi | PR:P06709 |
Family and domain databases
CDDi | cd16442, BPL, 1 hit |
DisProti | DP00349 |
Gene3Di | 1.10.10.10, 1 hit 3.30.930.10, 1 hit |
HAMAPi | MF_00978, Bifunct_BirA, 1 hit |
InterProi | View protein in InterPro IPR045864, aa-tRNA-synth_II/BPL/LPL IPR030855, Bifunct_BirA IPR004408, Biotin_CoA_COase_ligase IPR004409, Biotin_operon_repress_HTH IPR003142, BPL_C IPR004143, BPL_LPL_catalytic IPR013196, HTH_11 IPR008988, Transcriptional_repressor_C IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
Pfami | View protein in Pfam PF02237, BPL_C, 1 hit PF03099, BPL_LplA_LipB, 1 hit PF08279, HTH_11, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit SSF50037, SSF50037, 1 hit SSF55681, SSF55681, 1 hit |
TIGRFAMsi | TIGR00121, birA_ligase, 1 hit TIGR00122, birA_repr_reg, 1 hit |
PROSITEi | View protein in PROSITE PS51733, BPL_LPL_CATALYTIC, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | BIRA_ECOLI | |
Accessioni | P06709Primary (citable) accession number: P06709 Secondary accession number(s): Q2M8R4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | January 1, 1988 | |
Last modified: | February 23, 2022 | |
This is version 194 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- UniProtKB entry view manual
User manual for the UniProtKB entry view - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families