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Database: UniProt
Entry: C0QUW8_PERMH
LinkDB: C0QUW8_PERMH
Original site: C0QUW8_PERMH 
ID   C0QUW8_PERMH            Unreviewed;       222 AA.
AC   C0QUW8;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:ACO05010.1};
GN   OrderedLocusNames=PERMA_A0039 {ECO:0000313|EMBL:ACO05010.1};
OS   Persephonella marina (strain DSM 14350 / EX-H1).
OG   Plasmid pPERMA01 {ECO:0000313|Proteomes:UP000001366}.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Persephonella.
OX   NCBI_TaxID=123214 {ECO:0000313|EMBL:ACO05010.1, ECO:0000313|Proteomes:UP000001366};
RN   [1] {ECO:0000313|EMBL:ACO05010.1, ECO:0000313|Proteomes:UP000001366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14350 / EX-H1 {ECO:0000313|Proteomes:UP000001366};
RC   PLASMID=pPERMA01 {ECO:0000313|Proteomes:UP000001366};
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000256|ARBA:ARBA00009813}.
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DR   EMBL; CP001231; ACO05010.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0QUW8; -.
DR   PaxDb; 123214-PERMA_A0039; -.
DR   KEGG; pmx:PERMA_A0039; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_083593_1_1_0; -.
DR   Proteomes; UP000001366; Plasmid pPERMA01.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; Disulphide bond isomerase, DsbC/G, N-terminal; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR35272:SF3; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC; 1.
DR   PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Plasmid {ECO:0000313|EMBL:ACO05010.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001366};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..222
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002902570"
FT   DOMAIN          101..212
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13098"
SQ   SEQUENCE   222 AA;  24837 MW;  84F291EA26099332 CRC64;
     MKNSILGLLA CFSFSFAGVL EQTGAKIVEE KDLGDISQIV IQFPDGRKEV GYITKDNKYL
     IIGNVIDAKT GENITAKKYR ELDKVDVSKV PLDEAVKLKF GKGTKKLIMV ADPDCPFCKK
     AYQYLKNKDV EVYLFLFPLN IHPQAYDKSV KILCSKDPAK AYDKVESGNQ LQVSKCKEGE
     DKLKRHILIA NKLGVRGTPL FIDMQGHKIN GLNIPELEEA LK
//
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