Anaerobic dimethyl sulfoxide reductase chain B - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P18776 (DMSB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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

Names and origin

Protein names

Recommended name:
Anaerobic dimethyl sulfoxide reductase chain B

Alternative name(s):
DMSO reductase iron-sulfur subunit

Gene names

Name:	dmsB
Ordered Locus Names:	b0895, JW0878

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds.
Cofactor	Binds 4 4Fe-4S clusters.
Subunit structure	Heterotrimeric enzyme composed of a catalytic heterodimer (DmsAB) and a membrane anchor protein (DmsC).
Sequence similarities	Contains 3 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Biological process	Electron transport Transport
Domain	Repeat
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	anaerobic respiration Inferred from expression pattern PubMed 2544558. Source: EcoCyc electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	dimethyl sulfoxide reductase complex Inferred from direct assay PubMed 3280546. Source: EcoCyc
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from mutant phenotype Ref.6. Source: EcoCyc electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from mutant phenotype Ref.6. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1

Chain

2 – 205

204

Anaerobic dimethyl sulfoxide reductase chain B

PRO_0000159242

Regions

Domain

5 – 33

4Fe-4S ferredoxin-type 1

Domain

59 – 89

4Fe-4S ferredoxin-type 2

Domain

90 – 119

4Fe-4S ferredoxin-type 3

Sites

Metal binding

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 4 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 4 (4Fe-4S) By similarity

Metal binding

102

Iron-sulfur 4 (4Fe-4S) By similarity

Metal binding

105

Iron-sulfur 4 (4Fe-4S) By similarity

Metal binding

109

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

126

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

129

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

141

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

145

Iron-sulfur 1 (4Fe-4S) By similarity

Experimental info

Mutagenesis

102

C → F, S, W or Y: Loss of electron transfer from menaquinol to DMSO.

Sequence conflict

170

P → PRA in AAA83844. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P18776 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 7EC4417EED0809C6
Show »

FASTA

205

22,869

        10         20         30         40         50         60 
MTTQYGFFID SSRCTGCKTC ELACKDYKDL TPEVSFRRIY EYAGGDWQED NGVWHQNVFA 

        70         80         90        100        110        120 
YYLSISCNHC EDPACTKVCP SGAMHKREDG FVVVDEDVCI GCRYCHMACP YGAPQYNETK 

       130        140        150        160        170        180 
GHMTKCDGCY DRVAEGKKPI CVESCPLRAL DFGPIDELRK KHGDLAAVAP LPRAHFTKPN 

       190        200 
IVIKPNANSR PTGDTTGYLA NPKEV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli." Bilous P.T., Cole S.T., Anderson W.F., Weiner J.H. Mol. Microbiol. 2:785-795(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10. Strain: K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222.
[2]	"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.
[3]	"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.
[4]	"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.
[5]	"Electron paramagnetic resonance spectroscopic characterization of dimethyl sulfoxide reductase of Escherichia coli." Cammack R., Weiner J.H. Biochemistry 29:8410-8416(1990) [PubMed] [Europe PMC] [Abstract] Cited for: EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
[6]	"Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis." Rothery R.A., Weiner J.H. Biochemistry 30:8296-8305(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03412 Genomic DNA. Translation: AAA83844.1. U00096 Genomic DNA. Translation: AAC73981.1. AP009048 Genomic DNA. Translation: BAA35627.1.
PIR	F64828.
RefSeq	NP_415415.1. NC_000913.2. YP_489167.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P18776.
SMR	P18776. Positions 4-194.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9453N.
IntAct	P18776. 3 interactions.
STRING	511145.b0895.
Protein family/group databases
TCDB	5.A.3.3.2. prokaryotic molybdopterin-containing oxidoreductase (PMO) family.
Proteomic databases
PaxDb	P18776.
PRIDE	P18776.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73981; AAC73981; b0895. BAA35627; BAA35627; BAA35627.
GeneID	12931732. 945507.
KEGG	ecj:Y75_p0867. eco:b0895.
PATRIC	32117001. VBIEscCol129921_0925.
Organism-specific databases
EchoBASE	EB0229.
EcoGene	EG10233. dmsB.
Phylogenomic databases
eggNOG	COG0437.
HOGENOM	HOG000163387.
KO	K07307.
OMA	FTRPNIV.
ProtClustDB	CLSK879846.
Enzyme and pathway databases
BioCyc	EcoCyc:DMSB-MONOMER. ECOL316407:JW0878-MONOMER. MetaCyc:DMSB-MONOMER.
Gene expression databases
Genevestigator	P18776.
Family and domain databases
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR014297. DMSO_DmsB. [Graphical view]
Pfam	PF13247. Fer4_11. 1 hit. PF12797. Fer4_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR02951. DMSO_dmsB. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DMSB_ECOLI

Accession

Primary (citable) accession number: P18776
Secondary accession number(s): P77745

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 115 of the entry and version 4 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

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents