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Protein

Thiol-disulfide oxidoreductase ResA

Gene

resA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation.1 Publication

Pathwayi: cytochrome c assembly

This protein is involved in the pathway cytochrome c assembly, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway cytochrome c assembly and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cytochrome c-type biogenesis

Enzyme and pathway databases

BioCyciBSUB:BSU23150-MONOMER.
UniPathwayiUPA00555.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol-disulfide oxidoreductase ResA
Gene namesi
Name:resA
Synonyms:ypxA
Ordered Locus Names:BSU23150
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei11 – 30Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST20

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001201491 – 179Thiol-disulfide oxidoreductase ResAAdd BLAST179

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi74 ↔ 77Redox-active

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

DIPiDIP-61132N.

Structurei

Secondary structure

1179
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi46 – 48Combined sources3
Beta strandi54 – 56Combined sources3
Helixi57 – 60Combined sources4
Beta strandi63 – 70Combined sources8
Helixi75 – 91Combined sources17
Helixi92 – 94Combined sources3
Beta strandi96 – 104Combined sources9
Helixi107 – 117Combined sources11
Beta strandi123 – 126Combined sources4
Helixi130 – 134Combined sources5
Beta strandi142 – 146Combined sources5
Beta strandi150 – 158Combined sources9
Helixi162 – 172Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ST9X-ray1.50A/B37-179[»]
1SU9X-ray1.95A/B37-179[»]
2F9SX-ray1.40A/B37-179[»]
2H19X-ray2.00A/B37-179[»]
2H1AX-ray2.40A/B37-179[»]
2H1BX-ray1.95A/B/C/D37-179[»]
2H1DX-ray2.60A/B37-179[»]
2H1GX-ray3.10A/B37-179[»]
3C71X-ray1.90A37-179[»]
3C73X-ray2.50A/B40-179[»]
ProteinModelPortaliP35160.
SMRiP35160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35160.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 174ThioredoxinAdd BLAST139

Sequence similaritiesi

Belongs to the thioredoxin family. ResA subfamily.Curated
Contains 1 thioredoxin domain.Curated

Keywords - Domaini

Redox-active center, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000097217.
InParanoidiP35160.
OMAiMEIGKEA.
PhylomeDBiP35160.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_01319. ResA. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR023555. Thiol-dS_OxRdtase_ResA.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35160-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKKRRLFIR TGILLVLICA LGYTIYNAVF AGKESISEGS DAPNFVLEDT
60 70 80 90 100
NGKRIELSDL KGKGVFLNFW GTWCEPCKKE FPYMANQYKH FKSQGVEIVA
110 120 130 140 150
VNVGESKIAV HNFMKSYGVN FPVVLDTDRQ VLDAYDVSPL PTTFLINPEG
160 170
KVVKVVTGTM TESMIHDYMN LIKPGETSG
Length:179
Mass (Da):20,008
Last modified:August 29, 2003 - v2
Checksum:iE023A46F4BD702AC
GO

Sequence cautioni

The sequence AAA67494 differs from that shown. Reason: Frameshift at position 39.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09228 Genomic DNA. Translation: AAA67494.1. Frameshift.
AL009126 Genomic DNA. Translation: CAB14247.2.
PIRiS45556.
RefSeqiNP_390196.2. NC_000964.3.
WP_003230513.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14247; CAB14247; BSU23150.
GeneIDi938958.
KEGGibsu:BSU23150.
PATRICi18976447. VBIBacSub10457_2414.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09228 Genomic DNA. Translation: AAA67494.1. Frameshift.
AL009126 Genomic DNA. Translation: CAB14247.2.
PIRiS45556.
RefSeqiNP_390196.2. NC_000964.3.
WP_003230513.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ST9X-ray1.50A/B37-179[»]
1SU9X-ray1.95A/B37-179[»]
2F9SX-ray1.40A/B37-179[»]
2H19X-ray2.00A/B37-179[»]
2H1AX-ray2.40A/B37-179[»]
2H1BX-ray1.95A/B/C/D37-179[»]
2H1DX-ray2.60A/B37-179[»]
2H1GX-ray3.10A/B37-179[»]
3C71X-ray1.90A37-179[»]
3C73X-ray2.50A/B40-179[»]
ProteinModelPortaliP35160.
SMRiP35160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61132N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14247; CAB14247; BSU23150.
GeneIDi938958.
KEGGibsu:BSU23150.
PATRICi18976447. VBIBacSub10457_2414.

Phylogenomic databases

HOGENOMiHOG000097217.
InParanoidiP35160.
OMAiMEIGKEA.
PhylomeDBiP35160.

Enzyme and pathway databases

UniPathwayiUPA00555.
BioCyciBSUB:BSU23150-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP35160.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_01319. ResA. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR023555. Thiol-dS_OxRdtase_ResA.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRESA_BACSU
AccessioniPrimary (citable) accession number: P35160
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 29, 2003
Last modified: November 2, 2016
This is version 130 of the entry and version 2 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.