Reviewed, UniProtKB/Swiss-Prot P06709 (BIRA_ECOLI)

Names and origin

Protein names

Recommended name:
    Bifunctional protein birA
Including 2 domains:
  Recommended name:
      Biotin operon repressor
  Recommended name:
      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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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	Biotin DNA-binding
Molecular function	Ligase Repressor
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nanE	P0A761	1	EBI-545740,EBI-561432

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 321

321

Bifunctional protein birA

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)
	P06709-1 [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).

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

AP_003841.1.
NP_418404.1.

3D structure databases

PDBMSD

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	[»]

DisProt

DP00349.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9224N.

IntAct

P06709.

Genome annotation databases

GeneID

948469.

GenomeReviews

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

KEGG

ecj:JW3941.
eco:b3973.

Organism-specific databases

EchoBASE

EB0121.

EcoGene

EG10123. birA.

CMR

Search...

Phylogenomic databases

HOGENOM

P06709.

Enzyme and pathway databases

BioCyc

EcoCyc:BIOTINLIG-MON.

Family and domain databases

InterPro

IPR004408. BirA_CoA_COase_ligase.
IPR003142. BPL_C.
IPR004143. BPL_LipA_LipB.
IPR013196. HTH_11.
IPR004409. HTHbiotin_repres.
IPR011991. Wing_hlx_DNA_bd.
[Graphical view]

Gene3D

G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

PANTHER

PTHR12835. BirA_ligase. 1 hit.

Pfam

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

TIGRFAMs

TIGR00121. birA_ligase. 1 hit.
TIGR00122. birA_repr_reg. 1 hit.

ProDom

P06709.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

BindingDB

P06709.

LinkHub

P06709.

ProtoNet

Search...

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:	July 22, 2008
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)