P06709 (BIRA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein BirA

Including the following 2 domains:

1. Biotin operon repressor
2. Biotin--[acetyl-CoA-carboxylase] synthetase
   EC=6.3.4.15
   Alternative name(s):
   Biotin--protein ligase

Gene names

Name:	birA
Synonyms:	bioR, dhbB
Ordered Locus Names:	b3973, JW3941

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	BirA acts both as a biotin-operon repressor and as the enzyme that synthesizes the corepressor, acetyl-CoA:carbon-dioxide ligase. This protein also activates biotin to form biotinyl-5'-adenylate and transfers the biotin moiety to biotin-accepting proteins.
Catalytic activity	ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)].
Subunit structure	Monomer.
Sequence similarities	Belongs to the biotin--protein ligase family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Ligand	ATP-binding Biotin DNA-binding Nucleotide-binding
Molecular function	Ligase Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	biotin biosynthetic process Inferred from mutant phenotype. Source: EcoliWiki protein modification process Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred by curator. Source: EcoliWiki
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from direct assay. Source: EcoliWiki biotin-[acetyl-CoA-carboxylase] ligase activity Inferred from direct assay. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 321

321

Bifunctional protein BirA

PRO_0000064932

Regions

DNA binding

22 – 41

20

H-T-H motif

Natural variations

Natural variant

61

1

P → A in strain: RDD012.

Natural variant

70

1

K → E in strain: RDD012.

Secondary structure

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321

Helix Strand Turn

Details...

Helix

5 – 14

10

Helix

22 – 29

8

Helix

33 – 45

13

Beta strand

51 – 53

3

Turn

54 – 56

3

Beta strand

57 – 59

3

Helix

69 – 74

6

Beta strand

81 – 83

3

Beta strand

85 – 88

4

Helix

90 – 95

6

Helix

96 – 100

5

Beta strand

106 – 110

5

Beta strand

129 – 139

11

Helix

147 – 163

17

Beta strand

170 – 172

3

Turn

173 – 175

3

Beta strand

176 – 179

4

Beta strand

182 – 192

11

Beta strand

199 – 208

10

Turn

226 – 230

5

Helix

235 – 256

22

Helix

259 – 261

3

Helix

262 – 268

7

Turn

270 – 273

4

Beta strand

274 – 280

7

Beta strand

283 – 292

10

Beta strand

298 – 302

5

Beta strand

305 – 311

7

Beta strand

313 – 316

4

Sequences

	Sequence		Length	Mass (Da)
	P06709 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: B80AEBCEEE1BD2D4	FASTA	321	35,312
	10 20 30 40 50 60 MKDNTVPLKL IALLANGEFH SGEQLGETLG MSRAAINKHI QTLRDWGVDV FTVPGKGYSL 70 80 90 100 110 120 PEPIQLLNAK QILGQLDGGS VAVLPVIDST NQYLLDRIGE LKSGDACIAE YQQAGRGRRG 130 140 150 160 170 180 RKWFSPFGAN LYLSMFWRLE QGPAAAIGLS LVIGIVMAEV LRKLGADKVR VKWPNDLYLQ 190 200 210 220 230 240 DRKLAGILVE LTGKTGDAAQ IVIGAGINMA MRRVEESVVN QGWITLQEAG INLDRNTLAA 250 260 270 280 290 300 MLIRELRAAL ELFEQEGLAP YLSRWEKLDN FINRPVKLII GDKEIFGISR GIDKQGALLL 310 320 EQDGIIKPWM GGEISLRSAE K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the birA gene encoding the biotin operon repressor and biotin holoenzyme synthetase functions of Escherichia coli." Howard P.K., Shaw J., Otsuka A.J. Gene 35:321-331(1985) [PubMed: 3899863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of Escherichia coli." Buoncristiani M.R., Howard P.K., Otsuka A.J. Gene 44:255-261(1986) [PubMed: 3536662] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Cloning and identification of the Escherichia coli murB DNA sequence, which encodes UDP-N-acetylenolpyruvoylglucosamine reductase." Pucci M.J., Discotto L.F., Dougherty T.J. J. Bacteriol. 174:1690-1693(1992) [PubMed: 1311302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76. Strain: RDD012.
[7]	"Cloning, sequencing, and expression of the pantothenate kinase (coaA) gene of Escherichia coli." Song W.-J., Jackowski S. J. Bacteriol. 174:6411-6417(1992) [PubMed: 1328157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 226-321.
[8]	"Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains." Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W. Proc. Natl. Acad. Sci. U.S.A. 89:9257-9261(1992) [PubMed: 1409631] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[9]	"Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator." Weaver L.H., Kwon K., Beckett D., Matthews B.W. Proc. Natl. Acad. Sci. U.S.A. 98:6045-6050(2001) [PubMed: 11353844] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

BVECBF. B24029.

RefSeq

NP_418404.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
1K67	model	-	A	65-317	[»]
2EWN	X-ray	2.80	A/B	1-321	[»]

ProteinModelPortal

P06709.

SMR

P06709. Positions 3-320.

DisProt

DP00349.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9224N.

IntAct

P06709. 7 interactions.

MINT

MINT-1254106.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002534; EBESCP00000002534; EBESCG00000002070.
EBESCT00000014366; EBESCP00000013657; EBESCG00000013427.

GeneID

948469.

GenomeReviews

Gene locus JW3941 in contig AP009048_GR.
Gene locus b3973 in contig U00096_GR.

KEGG

ecj:JW3941.
eco:b3973.

PATRIC

32123467. VBIEscCol129921_4090.

Organism-specific databases

EchoBASE

EB0121.

EcoGene

EG10123. birA.

Phylogenomic databases

eggNOG

COG0340.

GeneTree

EBGT00050000011659.

HOGENOM

HBG750923.

OMA

VWKHIEE.

PhylomeDB

P06709.

ProtClustDB

PRK11886.

Enzyme and pathway databases

BioCyc

EcoCyc:BIOTINLIG-MONOMER.
MetaCyc:BIOTINLIG-MONOMER.

Gene expression databases

Genevestigator

P06709.

Family and domain databases

InterPro

IPR004408. Biotin_CoA_COase_ligase.
IPR004409. Biotin_operon_repress_HTH.
IPR003142. BPL_C.
IPR004143. BPL_LipA_LipB.
IPR013196. HTH_11.
IPR008988. Transcriptional_repressor_C.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K03524.

PANTHER

PTHR12835. BirA_ligase. 1 hit.

Pfam

PF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
PF08279. HTH_11. 1 hit.
[Graphical view]

SUPFAM

SSF50037. Transcr_rep_C. 1 hit.

TIGRFAMs

TIGR00121. BirA_ligase. 1 hit.
TIGR00122. BirA_repr_reg. 1 hit.

ProtoNet

Search...

Other

BindingDB

P06709.

Entry information

Entry name

BIRA_ECOLI

Accession

Primary (citable) accession number: P06709
Secondary accession number(s): Q2M8R4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	January 25, 2012
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program