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Q4QM23 (DSBD_HAEI8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thiol:disulfide interchange protein DsbD
EC=1.8.1.8
Alternative name(s):
Protein-disulfide reductase
Short name=Disulfide reductase
Gene names
Name:dsbD
Ordered Locus Names:NTHI1048
OrganismHaemophilus influenzae (strain 86-028NP) [Complete proteome] [HAMAP]
Taxonomic identifier281310 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps By similarity. HAMAP MF_00399

Catalytic activity

Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H. HAMAP MF_00399

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_00399.

Sequence similarities

Belongs to the thioredoxin family. DsbD subfamily.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 579563Thiol:disulfide interchange protein DsbD HAMAP MF_00399
PRO_0000304389

Regions

Transmembrane178 – 19821Helical; Potential
Transmembrane230 – 25021Helical; Potential
Transmembrane254 – 27421Helical; Potential
Transmembrane296 – 31621Helical; Potential
Transmembrane337 – 35721Helical; Potential
Transmembrane376 – 39621Helical; Potential
Transmembrane397 – 41721Helical; Potential
Transmembrane420 – 44021Helical; Potential
Domain449 – 579131Thioredoxin

Amino acid modifications

Disulfide bond124 ↔ 129Redox-active By similarity
Disulfide bond193 ↔ 315Redox-active By similarity
Disulfide bond495 ↔ 498Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4QM23 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 798E5E8CA5F029BA

FASTA57964,418
        10         20         30         40         50         60 
MKKLFLFFTL IFTAFAANSG LFDKKQTFLK VDDAFAFSAT LSTDKSQLQA HWDIADGYYL 

        70         80         90        100        110        120 
YQDKISAELV GKSNPLSLHT QQAAELHQDP YFGEVKVFTH SIDGIFRGTF NNADDKVEIT 

       130        140        150        160        170        180 
YQGCTEGFCY PPETKVLRIG DLAVSQEQIV EKTVEKNTAL LSEQDRLADG LFHSKWTIFG 

       190        200        210        220        230        240 
FFLLGLGLAF TPCVLPMLPL LSAIVIGQQQ RPNMMRAFSL AFLYVQGMAL TYTLLGLAVA 

       250        260        270        280        290        300 
AIGLPFQIAL QHPYVMIGLS ILFVALALSM FGLFTIQLPN SLQNKLNTWS QKQTSGAFGG 

       310        320        330        340        350        360 
AFAMGMIAGL VASPCTSAPL SGALLYVAQS GDLFTGAATL YLLALGMGVP LMLITLFGNK 

       370        380        390        400        410        420 
ILPKSGEWMN TVKQTFGFVM LALPVFLLSR ILPEVWEPRL WAGLATVFFI WFALQMSKNG 

       430        440        450        460        470        480 
FGYAIKIISF ALAMVTVQPL QNWIWQTQTT TQSAVENMPV SQVKFKQIKN TEELDRTLAE 

       490        500        510        520        530        540 
NPHSIAMLDL YADWCVACKE FEKLTFSDPQ VQQQFQNILL LQVNMTKNSP ENKALMERFN 

       550        560        570 
VMGLPTILFF DQQNNEIQGS RVTGFMDADA FSNWLKALH

« Hide

References

[1]"Genomic sequence of an otitis media isolate of nontypeable Haemophilus influenzae: comparative study with H. influenzae serotype d, strain KW20."
Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., Munson R.S. Jr.
J. Bacteriol. 187:4627-4636(2005) [PubMed: 15968074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 86-028NP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000057 Genomic DNA. Translation: AAX87924.1.
RefSeqYP_248584.1. NC_007146.2.

3D structure databases

HSSPHSSP built from PDB template 1L6P based on UniProtKB P36655.
ProteinModelPortalQ4QM23.
SMRQ4QM23. Positions 461-578.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4QM23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3430347.
GenomeReviewsGene locus NTHI1048 in contig CP000057_GR.
KEGGhit:NTHI1048.
PATRIC20182263. VBIHaeInf100748_0976.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4232.
HOGENOMHBG640883.
OMARILPEVW.
PhylomeDBQ4QM23.
ProtClustDBPRK00293.

Enzyme and pathway databases

BioCycHINF281310:NTHI1048-MONOMER.

Family and domain databases

HAMAPMF_00399. DbsD.
[Tree]
InterProIPR003834. Cyt_c_assmbl_TM_dom.
IPR022910. Thiol_diS_interchange_DbsD.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KOK04084.
PANTHERPTHR10438. Trx. 1 hit.
PfamPF02683. DsbD. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDSBD_HAEI8
AccessionPrimary (citable) accession number: Q4QM23
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 19, 2005
Last modified: January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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