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P35160

- RESA_BACSU

UniProt

P35160 - RESA_BACSU

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
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (29 Aug 2003)
      Previous versions | rss
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    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

    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-SubCell

    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.
    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

    MKKKRRLFIR TGILLVLICA LGYTIYNAVF AGKESISEGS DAPNFVLEDT    50
    NGKRIELSDL KGKGVFLNFW GTWCEPCKKE FPYMANQYKH FKSQGVEIVA 100
    VNVGESKIAV HNFMKSYGVN FPVVLDTDRQ VLDAYDVSPL PTTFLINPEG 150
    KVVKVVTGTM TESMIHDYMN LIKPGETSG 179
    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.
    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

    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 1, 2014
    This is version 115 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