ID K8WW48_9GAMM Unreviewed; 233 AA.
AC K8WW48;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=OOA_01762 {ECO:0000313|EMBL:EKT64823.1};
OS Providencia burhodogranariea DSM 19968.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT64823.1, ECO:0000313|Proteomes:UP000009336};
RN [1] {ECO:0000313|EMBL:EKT64823.1, ECO:0000313|Proteomes:UP000009336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT64823.1,
RC ECO:0000313|Proteomes:UP000009336};
RX PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA Galac M.R., Lazzaro B.P.;
RT "Comparative genomics of bacteria in the genus Providencia isolated from
RT wild Drosophila melanogaster.";
RL BMC Genomics 13:612-612(2012).
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:EKT64823.1}.
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DR EMBL; AKKL01000004; EKT64823.1; -; Genomic_DNA.
DR RefSeq; WP_008910401.1; NZ_KB233222.1.
DR AlphaFoldDB; K8WW48; -.
DR STRING; 1141662.OOA_01762; -.
DR PATRIC; fig|1141662.3.peg.358; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_083593_0_0_6; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000009336; 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 InterPro; IPR017937; Thioredoxin_CS.
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.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU364038};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 22..233
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5009999943"
FT DOMAIN 31..79
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 106..230
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 233 AA; 25602 MW; 81B1876156FB7B1D CRC64;
MKRKLLLWAA CIATFSVSVS AATDDKVIEE KLAKYNISVE SIKPSPIVGL NTVDTSDGII
YVTDDGKYLL QGPIYDLSGN APVNISNQPL MKKVEALKDE MIIFKAPKEK YVITVFTDIT
CGYCKKMHES IGELNSKGIT VRYLAYPRQG LEHESAKQMA SIWCNALPQS ALTKAFKGDE
VAIIDDCKID LSKHIKLGSQ FKMTGTPAIV LPDGQLLSGY LAPDSLLQLL EQK
//
