ID A0A0R0D3K1_9GAMM Unreviewed; 267 AA.
AC A0A0R0D3K1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=ABB27_02135 {ECO:0000313|EMBL:KRG72211.1};
OS Stenotrophomonas terrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=405446 {ECO:0000313|EMBL:KRG72211.1, ECO:0000313|Proteomes:UP000051863};
RN [1] {ECO:0000313|EMBL:KRG72211.1, ECO:0000313|Proteomes:UP000051863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18941 {ECO:0000313|EMBL:KRG72211.1,
RC ECO:0000313|Proteomes:UP000051863};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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:KRG72211.1}.
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DR EMBL; LDJJ01000006; KRG72211.1; -; Genomic_DNA.
DR RefSeq; WP_057626578.1; NZ_LDJJ01000006.1.
DR AlphaFoldDB; A0A0R0D3K1; -.
DR PATRIC; fig|405446.3.peg.3059; -.
DR OrthoDB; 5298214at2; -.
DR Proteomes; UP000051863; 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; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR PANTHER; PTHR35272:SF4; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBG; 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..21
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 22..267
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010000931"
FT DOMAIN 133..261
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 267 AA; 28016 MW; 7F4DEA199F52AB43 CRC64;
MMRSRSMLLF SLLALSPLAC AQTAGAPAST AGKPAAANEP AVVATLRSQG VEFMGTFETP
VGLTGYAGVA GQRPLGVYVS KDGQYAVVGT LVNAKGEDVS AAKLKELVSG PMGQQAWAKV
EASHWVRDGK ADAPRVIYSF SDPNCPYCNR FWEAAQPWVA AGKVQIRQIL VGVIREDSAN
KAAAILGASS PEQALIQNER DFAKGGIKPL ATVPAAVQAK LRANEALMLD LGFQGTPGIL
FKDADGTVQM RSGMPQGDDM QTVLGPR
//
