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P35160 (RESA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiol-disulfide oxidoreductase ResA
Gene names
Name:resA
Synonyms:ypxA
Ordered Locus Names:BSU23150
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Pathway

Protein modification; cytochrome c assembly. HAMAP-Rule MF_01319

Subcellular location

Cell membrane; Single-pass type II membrane protein. Note: The thioredoxin-like motif is exposed on the outside of the membrane. Ref.5

Sequence similarities

Belongs to the thioredoxin family. ResA subfamily.

Contains 1 thioredoxin domain.

Sequence caution

The sequence AAA67494.1 differs from that shown. Reason: Frameshift at position 39.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 179179Thiol-disulfide oxidoreductase ResA HAMAP-Rule MF_01319
PRO_0000120149

Regions

Transmembrane11 – 3020Helical; Signal-anchor for type II membrane protein; Probable
Domain36 – 174139Thioredoxin

Amino acid modifications

Disulfide bond74 ↔ 77Redox-active HAMAP-Rule MF_01319

Secondary structure

......................... 179
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35160 [UniParc].

Last modified August 29, 2003. Version 2.
Checksum: E023A46F4BD702AC

FASTA17920,008
        10         20         30         40         50         60 
MKKKRRLFIR TGILLVLICA LGYTIYNAVF AGKESISEGS DAPNFVLEDT NGKRIELSDL 

        70         80         90        100        110        120 
KGKGVFLNFW GTWCEPCKKE FPYMANQYKH FKSQGVEIVA VNVGESKIAV HNFMKSYGVN 

       130        140        150        160        170 
FPVVLDTDRQ VLDAYDVSPL PTTFLINPEG KVVKVVTGTM TESMIHDYMN LIKPGETSG 

« Hide

References

« Hide 'large scale' references
[1]"The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data."
Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.
Mol. Microbiol. 10:385-395(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Regulators of aerobic and anaerobic respiration in Bacillus subtilis."
Sun G., Sharkova E., Chesnut R., Birkey S., Duggan M.F., Sorokin A.V., Pujic P., Ehrlich S.D., Hulett F.M.
J. Bacteriol. 178:1374-1385(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE NAME.
[5]"Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis."
Erlendsson L.S., Acheson R.M., Hederstedt L., Le Brun N.E.
J. Biol. Chem. 278:17852-17858(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DETECTION OF FRAMESHIFT, FUNCTION, SUBCELLULAR LOCATION.
Strain: 168 / BGSC1A1.
[6]"Structural basis of redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA."
Crow A., Acheson R.M., Le Brun N.E., Oubrie A.
J. Biol. Chem. 279:23654-23660(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 37-179 IN THE OXIDIZED AND REDUCED STATES.
Strain: 168 / BGSC1A1.
[7]"Molecular basis for specificity of the extracytoplasmic thioredoxin ResA."
Lewin A., Crow A., Oubrie A., Le Brun N.E.
J. Biol. Chem. 281:35467-35477(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 37-179 WITH CYSTEINE MUTATIONS, CRYSTALLIZED AT HIGH PH.
Strain: 168 / BGSC1A1.
[8]"Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation."
Colbert C.L., Wu Q., Erbel P.J.A., Gardner K.H., Deisenhofer J.
Proc. Natl. Acad. Sci. U.S.A. 103:4410-4415(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 37-179, NMR.
Strain: 168 / BGSC1A1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L09228 Genomic DNA. Translation: AAA67494.1. Frameshift.
AL009126 Genomic DNA. Translation: CAB14247.2.
PIRS45556.
RefSeqNP_390196.2. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP35160.
SMRP35160. Positions 38-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU23150.

Proteomic databases

PaxDbP35160.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14247; CAB14247; BSU23150.
GeneID938958.
KEGGbsu:BSU23150.
PATRIC18976447. VBIBacSub10457_2414.

Organism-specific databases

GenoListBSU23150. [Micado]

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000097217.
OrthoDBEOG6GBMJ4.
PhylomeDBP35160.

Enzyme and pathway databases

BioCycBSUB:BSU23150-MONOMER.
UniPathwayUPA00555.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
HAMAPMF_01319. ResA.
InterProIPR000866. AhpC/TSA.
IPR023555. Thiol-dS_OxRdtase_ResA.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PfamPF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP35160.

Entry information

Entry nameRESA_BACSU
AccessionPrimary (citable) accession number: P35160
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 29, 2003
Last modified: July 9, 2014
This is version 114 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList