Disulfide bond formation protein B - Escherichia coli (strain K12)

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P0A6M2 (DSBB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Disulfide bond formation protein B

Alternative name(s):
Disulfide oxidoreductase

Gene names

Name:	dsbB
Synonyms:	roxB, ycgA
Ordered Locus Names:	b1185, JW5182

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. Ref.1 Ref.2
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.1 Ref.7.
Sequence similarities	Belongs to the DsbB family.
Sequence caution	The sequence AAA23711.1 differs from that shown. Reason: Erroneous initiation. The sequence AAA24220.1 differs from that shown. Reason: Frameshift at position 130.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Redox-active center Transmembrane Transmembrane helix
Molecular function	Chaperone Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: HAMAP protein disulfide oxidoreductase activity Inferred from mutant phenotype Ref.1. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dsbA	P0AEG4	1	EBI-1170740,EBI-549711

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 176

176

Disulfide bond formation protein B HAMAP-Rule MF_00286

PRO_0000059342

Regions

Topological domain

1 – 14

Cytoplasmic Probable

Transmembrane

15 – 31

Helical; Probable

Topological domain

32 – 49

Periplasmic Probable

Transmembrane

50 – 65

Helical; Probable

Topological domain

66 – 71

Cytoplasmic Probable

Transmembrane

72 – 89

Helical; Probable

Topological domain

90 – 144

Periplasmic Probable

Transmembrane

145 – 163

Helical; Probable

Topological domain

164 – 176

Cytoplasmic Probable

Amino acid modifications

Disulfide bond

41 ↔ 44

Redox-active Ref.8

Disulfide bond

104 ↔ 130

Redox-active Ref.8

Experimental info

Sequence conflict

M → MM Ref.6

Secondary structure

176

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6M2 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 9CBD673D51E9F09B
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FASTA

176

20,142

        10         20         30         40         50         60 
MLRFLNQCSQ GRGAWLLMAF TALALELTAL WFQHVMLLKP CVLCIYERCA LFGVLGAALI 

        70         80         90        100        110        120 
GAIAPKTPLR YVAMVIWLYS AFRGVQLTYE HTMLQLYPSP FATCDFMVRF PEWLPLDKWV 

       130        140        150        160        170 
PQVFVASGDC AERQWDFLGL EMPQWLLGIF IAYLIVAVLV VISQPFKAKK RDLFGR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A pathway for disulfide bond formation in vivo." Bardwell J.C.A., Lee J.-O., Jander G., Martin N., Belin D., Beckwith J. Proc. Natl. Acad. Sci. U.S.A. 90:1038-1042(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]	"Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo." Missiakas D., Georgopoulos C., Raina S. Proc. Natl. Acad. Sci. U.S.A. 90:7084-7088(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Cloning, sequencing, and expression of the nhaB gene, encoding a Na+/H+ antiporter in Escherichia coli." Pinner E., Padan E., Schuldiner S. J. Biol. Chem. 267:11064-11068(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-169. Strain: K12.
[7]	"Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation." Jander G., Martin N.L., Beckwith J. EMBO J. 13:5121-5127(1994) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF CYSTEINE RESIDUES.
[8]	"Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway." Kobayashi T., Ito K. EMBO J. 18:1192-1198(1999) [PubMed] [Europe PMC] [Abstract] Cited for: REDOX-ACTIVE SITES, DISULFIDE BONDS.
[9]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L03721 Genomic DNA. Translation: AAA23711.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74269.1.
AP009048 Genomic DNA. Translation: BAA36032.2.
M83655 Genomic DNA. Translation: AAA24220.1. Frameshift.

PIR

F64864.

RefSeq

NP_415703.3. NC_000913.2.
YP_489452.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HI7	X-ray	3.70	B	1-176	[»]
2K73	NMR	-	A	1-176	[»]
2K74	NMR	-	A	1-176	[»]
2LEG	NMR	-	B	1-176	[»]
2LTQ	NMR	-	A/D	1-176	[»]
2ZUP	X-ray	3.70	B	1-176	[»]
2ZUQ	X-ray	3.30	A/D	1-176	[»]
3E9J	X-ray	3.70	C/F	1-176	[»]

ProteinModelPortal

P0A6M2.

SMR

P0A6M2. Positions 1-176.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6M2. 1 interaction.

MINT

MINT-6742413.

STRING

511145.b1185.

Protein family/group databases

TCDB

5.A.2.1.1. disulfide bond oxidoreductase B (DsbB) family.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74269; AAC74269; b1185.
BAA36032; BAA36032; BAA36032.

GeneID

12932821.
946344.

KEGG

ecj:Y75_p1157.
eco:b1185.

PATRIC

32117616. VBIEscCol129921_1230.

Organism-specific databases

EchoBASE

EB1366.

EcoGene

EG11393. dsbB.

Phylogenomic databases

eggNOG

COG1495.

HOGENOM

HOG000218135.

K03611.

OMA

VLIAQPF.

ProtClustDB

PRK01749.

Enzyme and pathway databases

BioCyc

EcoCyc:DSBBPROT-MONOMER.
ECOL316407:JW5182-MONOMER.
MetaCyc:DSBBPROT-MONOMER.

Gene expression databases

Genevestigator

P0A6M2.

Family and domain databases

Gene3D

1.20.1550.10. 1 hit.

HAMAP

MF_00286. DsbB.

InterPro

IPR003752. DiS_bond_form_DsbB/BdbC.
IPR022920. Disulphide_bond_form_DsbB.
IPR023380. DsbB-like_dom.
[Graphical view]

Pfam

PF02600. DsbB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P0A6M2.

EvolutionaryTrace

P0A6M2.

Entry information

Entry name

DSBB_ECOLI

Accession

Primary (citable) accession number: P0A6M2
Secondary accession number(s): P30018, Q47408

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	May 10, 2005
Last modified:	May 29, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents