ID A0A1H7RN33_9GAMM Unreviewed; 230 AA.
AC A0A1H7RN33;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=SAMN05216262_11535 {ECO:0000313|EMBL:SEL61449.1};
OS Colwellia chukchiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=641665 {ECO:0000313|EMBL:SEL61449.1, ECO:0000313|Proteomes:UP000199297};
RN [1] {ECO:0000313|Proteomes:UP000199297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9127 {ECO:0000313|Proteomes:UP000199297};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FOBI01000015; SEL61449.1; -; Genomic_DNA.
DR RefSeq; WP_001228924.1; NZ_NBOC01000016.1.
DR AlphaFoldDB; A0A1H7RN33; -.
DR STRING; 641665.GCA_002104455_01377; -.
DR GeneID; 6803333; -.
DR OrthoDB; 9780340at2; -.
DR Proteomes; UP000199297; 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 Reference proteome {ECO:0000313|Proteomes:UP000199297};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 20..230
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5011329901"
FT DOMAIN 25..71
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 106..214
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 230 AA; 25139 MW; C473B94316B7B85D CRC64;
MRKLSPIILA LALSPLVQAE PVSEVSPVGK IDGMVSLPVT GMKAVESNGR IVFMSDSGRF
VIDGTLYDAW SKKPLTSLEE IREAGNTLDL SRLGLKMDDL NPLTLGEGKK KVVVFVDPRC
PHCHELLKQA LPLTKEYTFQ ILPVPVLGPD SERQVRQLGC ARDKKAATDA LLNGRIGNLE
QDDACNLEPM QRTLVTAQIL GIQGVPFIVA NDGRISRGRP YDLSAWLEGR
//
