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Protein

Bifunctional ligase/repressor BirA

Gene

birA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor.UniRule annotation

Catalytic activityi

ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)].UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei118BiotinUniRule annotation1
Binding sitei189BiotinUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi23 – 42H-T-H motifUniRule annotationAdd BLAST20

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Biotin, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional ligase/repressor BirAUniRule annotation
Alternative name(s):
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
Ordered Locus Names:BSU22440
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23G → S: Deregulation of biotin synthesis. 1 Publication1
Mutagenesisi38W → R: Deregulation of biotin synthesis. 1 Publication1
Mutagenesisi58G → E: Deregulation of biotin synthesis. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000649311 – 325Bifunctional ligase/repressor BirAAdd BLAST325

Proteomic databases

PaxDbiP0CI75.
PRIDEiP0CI75.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100012336.

Structurei

3D structure databases

ProteinModelPortaliP0CI75.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini74 – 262BPL/LPL catalyticPROSITE-ProRule annotationAdd BLAST189

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni122 – 124Biotin bindingUniRule annotation3

Sequence similaritiesi

Belongs to the biotin--protein ligase family.UniRule annotation
Contains 1 BPL/LPL catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105HJX. Bacteria.
COG0340. LUCA.
COG1654. LUCA.
HOGENOMiHOG000041811.
InParanoidiP0CI75.
KOiK03524.
OMAiDVCHVVL.
PhylomeDBiP0CI75.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_00978. Bifunct_BirA. 1 hit.
InterProiIPR030855. 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.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12835. PTHR12835. 1 hit.
PfamiPF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
PF08279. HTH_11. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50037. SSF50037. 1 hit.
TIGRFAMsiTIGR00121. birA_ligase. 1 hit.
TIGR00122. birA_repr_reg. 1 hit.
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CI75-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSTLRKDLI ELFSQAGNEF ISGQKISDAL GCSRTAVWKH IEELRKEGYE
60 70 80 90 100
VEAVRRKGYR LIKKPGKLSE SEIRFGLKTE VMGQHLIYHD VLSSTQKTAH
110 120 130 140 150
ELANNNAPEG TLVVADKQTA GRGRMSRVWH SQEGNGVWMS LILRPDIPLQ
160 170 180 190 200
KTPQLTLLAA VAVVQGIEEA AGIQTDIKWP NDILINGKKT VGILTEMQAE
210 220 230 240 250
EDRVRSVIIG IGINVNQQPN DFPDELKDIA TSLSQAAGEK IDRAGVIQHI
260 270 280 290 300
LLCFEKRYRD YMTHGFTPIK LLWESYALGI GTNMRARTLN GTFYGKALGI
310 320
DDEGVLLLET NEGIKKIYSA DIELG
Length:325
Mass (Da):36,182
Last modified:January 11, 2011 - v1
Checksum:i69088BB2CAD09221
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38424 Genomic DNA. Translation: AAA92879.1. Sequence problems.
L47709 Genomic DNA. Translation: AAB38447.1.
AL009126 Genomic DNA. Translation: CAB14160.1.
PIRiA69595.
RefSeqiNP_390125.1. NC_000964.3.
WP_003230650.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14160; CAB14160; BSU22440.
GeneIDi939028.
KEGGibsu:BSU22440.
PATRICi18976297. VBIBacSub10457_2339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38424 Genomic DNA. Translation: AAA92879.1. Sequence problems.
L47709 Genomic DNA. Translation: AAB38447.1.
AL009126 Genomic DNA. Translation: CAB14160.1.
PIRiA69595.
RefSeqiNP_390125.1. NC_000964.3.
WP_003230650.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP0CI75.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100012336.

Proteomic databases

PaxDbiP0CI75.
PRIDEiP0CI75.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14160; CAB14160; BSU22440.
GeneIDi939028.
KEGGibsu:BSU22440.
PATRICi18976297. VBIBacSub10457_2339.

Phylogenomic databases

eggNOGiENOG4105HJX. Bacteria.
COG0340. LUCA.
COG1654. LUCA.
HOGENOMiHOG000041811.
InParanoidiP0CI75.
KOiK03524.
OMAiDVCHVVL.
PhylomeDBiP0CI75.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_00978. Bifunct_BirA. 1 hit.
InterProiIPR030855. 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.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12835. PTHR12835. 1 hit.
PfamiPF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
PF08279. HTH_11. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50037. SSF50037. 1 hit.
TIGRFAMsiTIGR00121. birA_ligase. 1 hit.
TIGR00122. birA_repr_reg. 1 hit.
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBIRA_BACSU
AccessioniPrimary (citable) accession number: P0CI75
Secondary accession number(s): P42975
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: January 11, 2011
Last modified: October 5, 2016
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.