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Database: UniProt
Entry: R4YTJ6_OLEAN
LinkDB: R4YTJ6_OLEAN
Original site: R4YTJ6_OLEAN 
ID   R4YTJ6_OLEAN            Unreviewed;       263 AA.
AC   R4YTJ6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   28-FEB-2018, entry version 18.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   Name=dsbC {ECO:0000313|EMBL:CCK77053.1};
GN   ORFNames=OLEAN_C28770 {ECO:0000313|EMBL:CCK77053.1};
OS   Oleispira antarctica RB-8.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Oleispira.
OX   NCBI_TaxID=698738 {ECO:0000313|EMBL:CCK77053.1, ECO:0000313|Proteomes:UP000032749};
RN   [1] {ECO:0000313|EMBL:CCK77053.1, ECO:0000313|Proteomes:UP000032749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23877221; DOI=10.1038/ncomms3156;
RA   Kube M., Chernikova T.N., Al-Ramahi Y., Beloqui A., Lopez-Cortez N.,
RA   Guazzaroni M.E., Heipieper H.J., Klages S., Kotsyurbenko O.R.,
RA   Langer I., Nechitaylo T.Y., Lunsdorf H., Fernandez M., Juarez S.,
RA   Ciordia S., Singer A., Kagan O., Egorova O., Petit P.A., Stogios P.,
RA   Kim Y., Tchigvintsev A., Flick R., Denaro R., Genovese M., Albar J.P.,
RA   Reva O.N., Martinez-Gomariz M., Tran H., Ferrer M., Savchenko A.,
RA   Yakunin A.F., Yakimov M.M., Golyshina O.V., Reinhardt R.,
RA   Golyshin P.N.;
RT   "Genome sequence and functional genomic analysis of the oil-degrading
RT   bacterium Oleispira antarctica.";
RL   Nat. Commun. 4:2156-2156(2013).
CC   -!- FUNCTION: Required for disulfide bond formation in some
CC       periplasmic proteins. Acts by transferring its disulfide bond to
CC       other proteins and is reduced in the process.
CC       {ECO:0000256|RuleBase:RU364038}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU364038}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000256|RuleBase:RU364038}.
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DR   EMBL; FO203512; CCK77053.1; -; Genomic_DNA.
DR   RefSeq; WP_052718071.1; NZ_FO203512.1.
DR   EnsemblBacteria; CCK77053; CCK77053; OLEAN_C28770.
DR   KEGG; oai:OLEAN_C28770; -.
DR   PATRIC; fig|698738.3.peg.2988; -.
DR   KO; K03981; -.
DR   Proteomes; UP000032749; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000032749};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032749};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     19       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        20    263       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010005197.
FT   DOMAIN      128    259       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   263 AA;  28889 MW;  1A2725C054889A30 CRC64;
     MRILATLLAV FAVATTSYAA EVPQPAVDAA EQNKQLSLRV EAQISQSFGQ PVKVKEVMSL
     ANKQIIEAVL ADGSLVHLTP DLTHMVYRGE LYELLPLKPN NITKNRNNIK REGLMAALDD
     KDLVIFKAKG EEKTVINVFT DIDCGYCRKL HNEVARLNDL GITVRYLAYP RAGVTDRRTG
     QLTSSFKKIK SVWCDENRAE AMTAAKKNRT IKDNLDCDAP IAEHIALGYE VGVSGTPAIV
     LQDGRFIGGY MAADELAKTI GLN
//
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