ID A0A0W1CNG3_9SPHN Unreviewed; 247 AA.
AC A0A0W1CNG3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=ATE71_15570 {ECO:0000313|EMBL:KTE07354.1};
OS Sphingopyxis sp. H115.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759073 {ECO:0000313|EMBL:KTE07354.1, ECO:0000313|Proteomes:UP000054021};
RN [1] {ECO:0000313|EMBL:KTE07354.1, ECO:0000313|Proteomes:UP000054021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H115 {ECO:0000313|EMBL:KTE07354.1,
RC ECO:0000313|Proteomes:UP000054021};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be required for disulfide bond formation in some
CC proteins. {ECO:0000256|ARBA:ARBA00003565}.
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|RuleBase:RU364038}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {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:KTE07354.1}.
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DR EMBL; LNSA01000023; KTE07354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W1CNG3; -.
DR STRING; 1759073.ATE71_15570; -.
DR Proteomes; UP000054021; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd03020; DsbA_DsbC_DsbG; 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; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR PANTHER; PTHR35272:SF5; THIOREDOXIN-LIKE_FOLD DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF10411; DsbC_N; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:KTE07354.1};
KW Periplasm {ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Signal {ECO:0000256|RuleBase:RU364038}.
FT DOMAIN 43..242
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 247 AA; 26097 MW; FB227A18D3F100C4 CRC64;
MAAAALLASP VVCAQEKTEK VLLAKAAAEA EQQLKQTFTN LQFDDFEPAP VKGAIYQASA
GGRIVYYAPE SEHLLFASIF DKNGVNLTAL AQEAGISNRL KSIDSSQALE IGPKDAPTVI
EFTDPDCPYC RALNRYWAAK AAEGKPVRRL IFFVSGIHPE AAAKSEHILC SVDKAVAFKA
IYSGAAPTAL RTCAEGRGKV EAHAKVVSAA GVSGTPTLIA GGKLISGFQQ AEIEAFLSSA
KTNRVSR
//
