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Database: UniProt
Entry: A0A259EY91_9PROT
LinkDB: A0A259EY91_9PROT
Original site: A0A259EY91_9PROT 
ID   A0A259EY91_9PROT        Unreviewed;       282 AA.
AC   A0A259EY91;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=B7X93_00300 {ECO:0000313|EMBL:OZA31229.1};
OS   Hydrogenophilales bacterium 17-61-9.
OC   Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX   NCBI_TaxID=1970524 {ECO:0000313|EMBL:OZA31229.1, ECO:0000313|Proteomes:UP000215711};
RN   [1] {ECO:0000313|EMBL:OZA31229.1, ECO:0000313|Proteomes:UP000215711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17-61-9 {ECO:0000313|EMBL:OZA31229.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC       proteins. Acts by transferring its disulfide bond to other proteins and
CC       is reduced in the process. {ECO:0000256|RuleBase:RU364038}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC       ECO:0000256|RuleBase:RU364038}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000256|ARBA:ARBA00009813, ECO:0000256|RuleBase:RU364038}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZA31229.1}.
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DR   EMBL; NCIF01000002; OZA31229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259EY91; -.
DR   Proteomes; UP000215711; 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; 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; 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   PANTHER; PTHR35272:SF3; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC; 1.
DR   PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF54423; DsbC/DsbG N-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|RuleBase:RU364038"
FT   CHAIN           26..282
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|RuleBase:RU364038"
FT                   /id="PRO_5011809378"
FT   DOMAIN          57..109
FT                   /note="Disulphide bond isomerase DsbC/G N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10411"
FT   DOMAIN          143..266
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13098"
SQ   SEQUENCE   282 AA;  30418 MW;  D823775F12DDB616 CRC64;
     MRHLKMKSIL TNLLVLYFAS GAALAQEAVD PQSQIDAIAK AGGAQRAAHQ AELAAVQKNL
     RLMYPKTRFE KISPTPVPGI YEVVMGRNVA FVEESGRYFI FGRLFDMEQQ QDITSESQAA
     AQPASTKVNF SILPLDQAIK SVRGNGRRAL AVFSDPDCPY CKKLEQELGK VEDVTIYTFL
     MPLDQLHPEA RAKADAVWCS KDRSAAWSAL MLEGKVPRKV KGCGAPHNVV LPLAKKLGIN
     GTPFLIASDG RTMPGAAPAA RLSAWLDAGA KPVTSNGKGG AQ
//
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