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Protein

Anaerobic dimethyl sulfoxide reductase chain B

Gene

dmsB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds.

Cofactori

[4Fe-4S] clusterNote: Binds 4 [4Fe-4S] clusters.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi14Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi17Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi20Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi24Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi67Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi70Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi75Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi79Iron-sulfur 4 (4Fe-4S)By similarity1
Metal bindingi99Iron-sulfur 4 (4Fe-4S)By similarity1
Metal bindingi102Iron-sulfur 4 (4Fe-4S)By similarity1
Metal bindingi105Iron-sulfur 4 (4Fe-4S)By similarity1
Metal bindingi109Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi126Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi129Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi141Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi145Iron-sulfur 1 (4Fe-4S)By similarity1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • dimethyl sulfoxide reductase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:DMSB-MONOMER.
ECOL316407:JW0878-MONOMER.
MetaCyc:DMSB-MONOMER.

Protein family/group databases

TCDBi5.A.3.3.2. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaerobic dimethyl sulfoxide reductase chain B
Alternative name(s):
DMSO reductase iron-sulfur subunit
Gene namesi
Name:dmsB
Ordered Locus Names:b0895, JW0878
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10233. dmsB.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • dimethyl sulfoxide reductase complex Source: EcoCyc
  • intrinsic component of periplasmic side of plasma membrane Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi102C → F, S, W or Y: Loss of electron transfer from menaquinol to DMSO. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001592422 – 205Anaerobic dimethyl sulfoxide reductase chain BAdd BLAST204

Proteomic databases

PaxDbiP18776.
PRIDEiP18776.

Interactioni

Subunit structurei

Heterotrimeric enzyme composed of a catalytic heterodimer (DmsAB) and a membrane anchor protein (DmsC).

Binary interactionsi

WithEntry#Exp.IntActNotes
dmsAP187752EBI-1120825,EBI-4411104

Protein-protein interaction databases

DIPiDIP-9453N.
IntActiP18776. 6 interactors.
STRINGi511145.b0895.

Structurei

3D structure databases

ProteinModelPortaliP18776.
SMRiP18776.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 334Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST29
Domaini59 – 894Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST31
Domaini90 – 1194Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST30

Sequence similaritiesi

Contains 3 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105QAX. Bacteria.
COG0437. LUCA.
HOGENOMiHOG000163387.
InParanoidiP18776.
KOiK07307.
OMAiFKRHFDI.
PhylomeDBiP18776.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR014297. DMSO_DmsB.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
PF12800. Fer4_4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02951. DMSO_dmsB. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18776-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTQYGFFID SSRCTGCKTC ELACKDYKDL TPEVSFRRIY EYAGGDWQED
60 70 80 90 100
NGVWHQNVFA YYLSISCNHC EDPACTKVCP SGAMHKREDG FVVVDEDVCI
110 120 130 140 150
GCRYCHMACP YGAPQYNETK GHMTKCDGCY DRVAEGKKPI CVESCPLRAL
160 170 180 190 200
DFGPIDELRK KHGDLAAVAP LPRAHFTKPN IVIKPNANSR PTGDTTGYLA

NPKEV
Length:205
Mass (Da):22,869
Last modified:January 23, 2007 - v4
Checksum:i7EC4417EED0809C6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti170P → PRA in AAA83844 (PubMed:3062312).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03412 Genomic DNA. Translation: AAA83844.1.
U00096 Genomic DNA. Translation: AAC73981.1.
AP009048 Genomic DNA. Translation: BAA35627.1.
PIRiF64828.
RefSeqiNP_415415.1. NC_000913.3.
WP_000213098.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73981; AAC73981; b0895.
BAA35627; BAA35627; BAA35627.
GeneIDi945507.
KEGGiecj:JW0878.
eco:b0895.
PATRICi32117001. VBIEscCol129921_0925.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03412 Genomic DNA. Translation: AAA83844.1.
U00096 Genomic DNA. Translation: AAC73981.1.
AP009048 Genomic DNA. Translation: BAA35627.1.
PIRiF64828.
RefSeqiNP_415415.1. NC_000913.3.
WP_000213098.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP18776.
SMRiP18776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9453N.
IntActiP18776. 6 interactors.
STRINGi511145.b0895.

Protein family/group databases

TCDBi5.A.3.3.2. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PaxDbiP18776.
PRIDEiP18776.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73981; AAC73981; b0895.
BAA35627; BAA35627; BAA35627.
GeneIDi945507.
KEGGiecj:JW0878.
eco:b0895.
PATRICi32117001. VBIEscCol129921_0925.

Organism-specific databases

EchoBASEiEB0229.
EcoGeneiEG10233. dmsB.

Phylogenomic databases

eggNOGiENOG4105QAX. Bacteria.
COG0437. LUCA.
HOGENOMiHOG000163387.
InParanoidiP18776.
KOiK07307.
OMAiFKRHFDI.
PhylomeDBiP18776.

Enzyme and pathway databases

BioCyciEcoCyc:DMSB-MONOMER.
ECOL316407:JW0878-MONOMER.
MetaCyc:DMSB-MONOMER.

Miscellaneous databases

PROiP18776.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR014297. DMSO_DmsB.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
PF12800. Fer4_4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02951. DMSO_dmsB. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDMSB_ECOLI
AccessioniPrimary (citable) accession number: P18776
Secondary accession number(s): P77745
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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