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Database: UniProt
Entry: H1G2I4_9GAMM
LinkDB: H1G2I4_9GAMM
Original site: H1G2I4_9GAMM 
ID   H1G2I4_9GAMM            Unreviewed;       245 AA.
AC   H1G2I4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   25-APR-2018, entry version 24.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=ECTPHS_04970 {ECO:0000313|EMBL:EHQ52021.1};
OS   Ectothiorhodospira sp. PHS-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ52021.1, ECO:0000313|Proteomes:UP000005314};
RN   [1] {ECO:0000313|EMBL:EHQ52021.1, ECO:0000313|Proteomes:UP000005314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ52021.1,
RC   ECO:0000313|Proteomes:UP000005314};
RA   Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA   Hoeft S., Oremland R.S., Stolz J.;
RT   "ArxA, a new clade of arsenite oxidase within the DMSO family of
RT   molybdenum oxidoreductases.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHQ52021.1}.
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DR   EMBL; AGBG01000008; EHQ52021.1; -; Genomic_DNA.
DR   RefSeq; WP_008931588.1; NZ_AGBG01000008.1.
DR   EnsemblBacteria; EHQ52021; EHQ52021; ECTPHS_04970.
DR   PATRIC; fig|519989.5.peg.988; -.
DR   OrthoDB; POG091H04JN; -.
DR   BioCyc; ESP519989:G10UP-996-MONOMER; -.
DR   Proteomes; UP000005314; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005314};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005314};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     20       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        21    245       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010005176.
FT   DOMAIN       32     84       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      114    234       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   245 AA;  27142 MW;  B3CD674E182B3C7D CRC64;
     MYRYGLSLVL VILLAVPAMA GADAQIQRQL KERVSLLVPN AEPTSIQETP VKGLYEVRYG
     AQLFYISADG QYVLDGELVE LDTRRSLTAA SRSLGRREML TEMDEAGMVV YAPKGRTEHV
     ITVFTDVDCP YCRRLHEEVP ALTEQGVKVR YAMFPRSGEG SPTFRKMVGI WCADDRAKAM
     DQVKDGKNVT EKTCDTPVME HVIMGQMMGI NGTPAILLES GDLIPGYRPA GDIMEMIRHV
     KAAAQ
//
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