ID A0A1M4WS35_9GAMM Unreviewed; 250 AA.
AC A0A1M4WS35;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=SAMN04487965_0765 {ECO:0000313|EMBL:SHE84101.1};
OS Microbulbifer donghaiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=494016 {ECO:0000313|EMBL:SHE84101.1, ECO:0000313|Proteomes:UP000184170};
RN [1] {ECO:0000313|EMBL:SHE84101.1, ECO:0000313|Proteomes:UP000184170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7063 {ECO:0000313|EMBL:SHE84101.1,
RC ECO:0000313|Proteomes:UP000184170};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQVA01000001; SHE84101.1; -; Genomic_DNA.
DR RefSeq; WP_073271620.1; NZ_FQVA01000001.1.
DR AlphaFoldDB; A0A1M4WS35; -.
DR STRING; 494016.SAMN04487965_0765; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000184170; 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..24
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 25..250
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5011817429"
FT DOMAIN 35..88
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 123..248
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 250 AA; 27205 MW; 8D5A9865CFD29F4C CRC64;
MTLFNKPLML VGALFALLGA TAQAEVDAEV AKTIKARLEA GNPKASYGEV RESPISGLYE
VDVDGGANTL FVSADGSHFI FGDLYQVHAG GGLANISEQR RTTKRAAIMD AQNVDDMIVF
SPKGETKAHI YVFTDVDCGY CRKLHNDVPE LNKRGIEVRY LAFPRTGLNS LGYRKIATAW
CAEDRNKTLT ALKNRENVPL KVCKNNPVAE QYNLGNDVID VRGTPTIVMQ DGSVVPGYLP
PETMIKALGI
//
