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P35160

- RESA_BACSU

UniProt

P35160 - RESA_BACSU

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Protein

Thiol-disulfide oxidoreductase ResA

Gene

resA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

GO - Molecular functioni

  1. antioxidant activity Source: InterPro
  2. disulfide oxidoreductase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cell redox homeostasis Source: UniProtKB-HAMAP
  2. cytochrome complex assembly Source: UniProtKB-HAMAP
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
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU23150. [Micado]

Subcellular locationi

Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication
Note: The thioredoxin-like motif is exposed on the outside of the membrane.

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 179179Thiol-disulfide oxidoreductase ResAPRO_0000120149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi74 ↔ 77Redox-active

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP35160.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU23150.

Structurei

Secondary structure

1
179
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi46 – 483
Beta strandi54 – 563
Helixi57 – 604
Beta strandi63 – 708
Helixi75 – 9117
Helixi92 – 943
Beta strandi96 – 1049
Helixi107 – 11711
Beta strandi123 – 1264
Helixi130 – 1345
Beta strandi142 – 1465
Beta strandi150 – 1589
Helixi162 – 17211

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 38-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35160.

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3020Helical; Signal-anchor for type II membrane proteinCuratedAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 174139ThioredoxinAdd
BLAST

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

eggNOGiCOG0526.
HOGENOMiHOG000097217.
InParanoidiP35160.
OrthoDBiEOG6GBMJ4.
PhylomeDBiP35160.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_01319. ResA.
InterProiIPR000866. AhpC/TSA.
IPR023555. Thiol-dS_OxRdtase_ResA.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[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 AAA67494.1 differs from that shown. Reason: Frameshift at position 39.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L09228 Genomic DNA. Translation: AAA67494.1. Frameshift.
AL009126 Genomic DNA. Translation: CAB14247.2.
PIRiS45556.
RefSeqiNP_390196.2. NC_000964.3.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L09228 Genomic DNA. Translation: AAA67494.1 . Frameshift.
AL009126 Genomic DNA. Translation: CAB14247.2 .
PIRi S45556.
RefSeqi NP_390196.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ST9 X-ray 1.50 A/B 37-179 [» ]
1SU9 X-ray 1.95 A/B 37-179 [» ]
2F9S X-ray 1.40 A/B 37-179 [» ]
2H19 X-ray 2.00 A/B 37-179 [» ]
2H1A X-ray 2.40 A/B 37-179 [» ]
2H1B X-ray 1.95 A/B/C/D 37-179 [» ]
2H1D X-ray 2.60 A/B 37-179 [» ]
2H1G X-ray 3.10 A/B 37-179 [» ]
3C71 X-ray 1.90 A 37-179 [» ]
3C73 X-ray 2.50 A/B 40-179 [» ]
ProteinModelPortali P35160.
SMRi P35160. Positions 38-175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU23150.

Proteomic databases

PaxDbi P35160.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14247 ; CAB14247 ; BSU23150 .
GeneIDi 938958.
KEGGi bsu:BSU23150.
PATRICi 18976447. VBIBacSub10457_2414.

Organism-specific databases

GenoListi BSU23150. [Micado ]

Phylogenomic databases

eggNOGi COG0526.
HOGENOMi HOG000097217.
InParanoidi P35160.
OrthoDBi EOG6GBMJ4.
PhylomeDBi P35160.

Enzyme and pathway databases

UniPathwayi UPA00555 .
BioCyci BSUB:BSU23150-MONOMER.

Miscellaneous databases

EvolutionaryTracei P35160.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
HAMAPi MF_01319. ResA.
InterProi IPR000866. AhpC/TSA.
IPR023555. Thiol-dS_OxRdtase_ResA.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view ]
Pfami PF00578. AhpC-TSA. 1 hit.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

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: October 29, 2014
This is version 116 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

External Data

Dasty 3