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Database: UniProt
Entry: B0VME8_ACIBS
LinkDB: B0VME8_ACIBS
Original site: B0VME8_ACIBS 
ID   B0VME8_ACIBS            Unreviewed;       271 AA.
AC   B0VME8;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   20-JUN-2018, entry version 62.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   Name=dsbC {ECO:0000313|EMBL:CAP02562.1};
GN   OrderedLocusNames=ABSDF3293 {ECO:0000313|EMBL:CAP02562.1};
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP02562.1, ECO:0000313|Proteomes:UP000001741};
RN   [1] {ECO:0000313|EMBL:CAP02562.1, ECO:0000313|Proteomes:UP000001741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF {ECO:0000313|EMBL:CAP02562.1,
RC   ECO:0000313|Proteomes:UP000001741};
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S.,
RA   Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S.,
RA   Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M.,
RA   Raoult D., Medigue C., Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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; CU468230; CAP02562.1; -; Genomic_DNA.
DR   ProteinModelPortal; B0VME8; -.
DR   EnsemblBacteria; CAP02562; CAP02562; ABSDF3293.
DR   KEGG; abm:ABSDF3293; -.
DR   HOGENOM; HOG000222077; -.
DR   KO; K03981; -.
DR   OMA; QMIVYKA; -.
DR   Proteomes; UP000001741; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; -; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR   InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001741};
KW   Isomerase {ECO:0000313|EMBL:CAP02562.1};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     21       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        22    271       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5002755521.
FT   DOMAIN      133    271       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   COILED       51     78       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   271 AA;  30132 MW;  651EC36A86032271 CRC64;
     MSFTRSQIFL ACALASSLLF SACSKENKPQ KEDALTATAP ATGEASTIIE RNAKQRLIET
     LQKQFKNANI NVKILDIKPT EVPNLYWVNL EGMTSVYTTS DGKYLIQGDV IRLGGKELHN
     IGDSLQASEN KKHLAALKNE DLIAYPAKGG KAKHVIYVFT DVSCPYCHKL HEHLAEINEK
     SIEVRYIAWP RGEQFMPTME AVWCSADRKA AFNQAVQGIN IPPAQCKNPV REQYQLGLNM
     GVNGTPAIYN VDGEYLGGYL TPDELIKRLD K
//
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