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Protein

Thiol:disulfide interchange protein DsbC

Gene

dsbC

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein. Also acts as a disulfide isomerase (By similarity).By similarity

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol:disulfide interchange protein DsbC
Gene namesi
Name:dsbC
Synonyms:xprA
Ordered Locus Names:HI_1213
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 229211Thiol:disulfide interchange protein DsbCPRO_0000034276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi116 ↔ 119Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi71421.HI1213.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni21 – 233Combined sources
Helixi24 – 285Combined sources
Turni29 – 313Combined sources
Beta strandi56 – 627Combined sources
Turni73 – 753Combined sources
Helixi81 – 9010Combined sources
Helixi91 – 955Combined sources
Beta strandi96 – 994Combined sources
Beta strandi105 – 1128Combined sources
Helixi117 – 1237Combined sources
Helixi126 – 1316Combined sources
Beta strandi134 – 1407Combined sources
Helixi149 – 15911Combined sources
Beta strandi160 – 1623Combined sources
Helixi163 – 1719Combined sources
Helixi184 – 19512Combined sources
Beta strandi202 – 2043Combined sources
Helixi217 – 22610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3BX-ray2.50A19-229[»]
ProteinModelPortaliP45111.
SMRiP45111. Positions 20-228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45111.

Family & Domainsi

Sequence similaritiesi

Belongs to the thioredoxin family. DsbC subfamily.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiENOG4105T95. Bacteria.
COG1651. LUCA.
KOiK03981.
OMAiKNEMIVY.
OrthoDBiEOG632D3W.
PhylomeDBiP45111.

Family and domain databases

Gene3Di3.10.450.70. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR018950. DiS-bond_isomerase_DsbC/G_N.
IPR009094. DiS-bond_isomerase_DsbC_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10411. DsbC_N. 1 hit.
PF13098. Thioredoxin_2. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF54423. SSF54423. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P45111-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIFTALLC VAAANAMADD AAIKRKLQSF NISNIVIKSS PISGIKTAVT
60 70 80 90 100
DQGILYVSED GKYLFEGKLY ELTNNGPVDV AGKILVDKLN SYKDEMIVYP
110 120 130 140 150
AKNEKHVVTV FMDITCHYCH LLHQQLKEYN DLGITVRYLA FPRAGMNNQT
160 170 180 190 200
AKQMEAIWTA KDPVFALNEA EKGNLPKEVK TPNIVKKHYE LGIQFGVRGT
210 220
PSIVTSTGEL IGGYLKPADL LRALEETAQ
Length:229
Mass (Da):25,351
Last modified:November 1, 1995 - v1
Checksum:iAF0F08AFC0FD08E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22866.1.
PIRiE64110.
RefSeqiNP_439369.1. NC_000907.1.
WP_005647404.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22866; AAC22866; HI_1213.
GeneIDi950655.
KEGGihin:HI1213.
PATRICi20191105. VBIHaeInf48452_1265.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22866.1.
PIRiE64110.
RefSeqiNP_439369.1. NC_000907.1.
WP_005647404.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3BX-ray2.50A19-229[»]
ProteinModelPortaliP45111.
SMRiP45111. Positions 20-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI1213.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22866; AAC22866; HI_1213.
GeneIDi950655.
KEGGihin:HI1213.
PATRICi20191105. VBIHaeInf48452_1265.

Phylogenomic databases

eggNOGiENOG4105T95. Bacteria.
COG1651. LUCA.
KOiK03981.
OMAiKNEMIVY.
OrthoDBiEOG632D3W.
PhylomeDBiP45111.

Miscellaneous databases

EvolutionaryTraceiP45111.

Family and domain databases

Gene3Di3.10.450.70. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR018950. DiS-bond_isomerase_DsbC/G_N.
IPR009094. DiS-bond_isomerase_DsbC_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10411. DsbC_N. 1 hit.
PF13098. Thioredoxin_2. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF54423. SSF54423. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-229, SUBUNIT, DISULFIDE BOND.

Entry informationi

Entry nameiDSBC_HAEIN
AccessioniPrimary (citable) accession number: P45111
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 11, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.