ID A0A241WK33_9GAMM Unreviewed; 240 AA.
AC A0A241WK33;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=B9T35_07000 {ECO:0000313|EMBL:OTG94151.1};
OS Acinetobacter sp. ANC 3832.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1977874 {ECO:0000313|EMBL:OTG94151.1, ECO:0000313|Proteomes:UP000194704};
RN [1] {ECO:0000313|EMBL:OTG94151.1, ECO:0000313|Proteomes:UP000194704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 3832 {ECO:0000313|EMBL:OTG94151.1,
RC ECO:0000313|Proteomes:UP000194704};
RA Nemec A., Radolfova-Krizova L.;
RT "High diversity of culturable Acinetobacter species in natural soil and
RT water ecosystems.";
RL Submitted (APR-2017) 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:OTG94151.1}.
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DR EMBL; NEGJ01000004; OTG94151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A241WK33; -.
DR STRING; 1977874.B9T35_07000; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000194704; 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..22
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 23..240
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5011812737"
FT DOMAIN 28..80
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 110..229
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 240 AA; 27310 MW; 5366841DBADE88F4 CRC64;
MKKSQILISI FVSLLCNQMS LANTESIKNM AQSFPLKMKP EFIDKTPIDN IYILSNPRGS
FLIDASSRYL IQGDIIDLKT DLNITEAVYQ SHYSINPKQL PVAQAFKEIK GNGKRLLYVF
SDPDCPACQL LQSELEDVDD ITIYTFPFAL THLHPTAVET AKKIWCSKEP LKVWKSYLIE
QQKPQNNSMS CINPIDKNME LAKLHKIALT PTIFNSLGHR ISGVPDLNQL EEFINTKKYD
//
