ID A0A0J5LXG8_PLUGE Unreviewed; 248 AA.
AC A0A0J5LXG8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN Name=dsbG {ECO:0000313|EMBL:KMK14178.1};
GN ORFNames=ABW06_09945 {ECO:0000313|EMBL:KMK14178.1};
OS Pluralibacter gergoviae (Enterobacter gergoviae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK14178.1, ECO:0000313|Proteomes:UP000036196};
RN [1] {ECO:0000313|EMBL:KMK14178.1, ECO:0000313|Proteomes:UP000036196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS81F13 {ECO:0000313|EMBL:KMK14178.1,
RC ECO:0000313|Proteomes:UP000036196};
RA Greninger A.L., Miller S.;
RT "Genome sequences of Pluralibacter gergoviae.";
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:KMK14178.1}.
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DR EMBL; LDZF01000008; KMK14178.1; -; Genomic_DNA.
DR RefSeq; WP_048278876.1; NZ_VWRP01000022.1.
DR AlphaFoldDB; A0A0J5LXG8; -.
DR STRING; 61647.LG71_21870; -.
DR PATRIC; fig|61647.15.peg.5359; -.
DR eggNOG; COG1651; Bacteria.
DR Proteomes; UP000036196; 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; 3.10.450.70; 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 Isomerase {ECO:0000313|EMBL:KMK14178.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000036196};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 18..248
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010005242"
FT DOMAIN 111..244
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 248 AA; 27240 MW; C2681FDBCEA30C59 CRC64;
MSRFALACCL LPAIAQADDL PAPVKAIEKQ GITIIKSFDA PGGMKGYLGK YQDMGVTIYL
TPDGKQAISG YMYDAKGTNL SEQMIQQELY GPQGRALWQQ MEKSTWLLDG KKEAPRIIYV
FSDPFCPYCR QFWQMARPWV ESGKVQLRTL LVGVIKPESP ATAAAILASS DPAKTWHDYE
QSGGKLKLTV PASAAPAQMK VLHDNEKLMD TLGASATPAI YYLNDQQMLQ QVAGLPDAEN
LQAMMGDK
//
