ID A0A385C6D4_9GAMM Unreviewed; 253 AA.
AC A0A385C6D4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN Name=dsbG {ECO:0000313|EMBL:AXQ22623.1};
GN ORFNames=BEN71_11300 {ECO:0000313|EMBL:AXQ22623.1};
OS Acinetobacter wuhouensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1879050 {ECO:0000313|EMBL:AXQ22623.1, ECO:0000313|Proteomes:UP000257257};
RN [1] {ECO:0000313|EMBL:AXQ22623.1, ECO:0000313|Proteomes:UP000257257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHA60 {ECO:0000313|EMBL:AXQ22623.1,
RC ECO:0000313|Proteomes:UP000257257};
RX PubMed=30117799; DOI=10.1099/ijsem.0.002963;
RA Hu Y., Feng Y., Qin J., Radolfova-Krizova L., Maixnerova M., Zhang X.,
RA Nemec A., Zong Z.;
RT "Acinetobacter wuhouensis sp. nov., isolated from hospital sewage.";
RL Int. J. Syst. Evol. Microbiol. 68:3212-3216(2018).
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; CP031716; AXQ22623.1; -; Genomic_DNA.
DR RefSeq; WP_068973146.1; NZ_CP031716.1.
DR AlphaFoldDB; A0A385C6D4; -.
DR STRING; 1879050.GCA_001696605_00434; -.
DR KEGG; awu:BEN71_11300; -.
DR OrthoDB; 5298214at2; -.
DR Proteomes; UP000257257; Chromosome.
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..25
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 26..253
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5017105892"
FT DOMAIN 120..242
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 253 AA; 28552 MW; 8CC50FA29D342D36 CRC64;
MNLKKLSLYS LTSSLMLLMS SSVFSANTDV IKNKLEKEGY RFVQQIDAPE GLEGWTGYRD
EYPSTVFISK DRKHYIVGDL YDASGKNLSE EAINTHVKGA VLDEIWKSLE KSAWIQDGDS
NAKKIIYVFN DPNCPYCHTF WKQARPFVES GKVQLRHILV GVIRPSSKGQ AATILNSANP
AEVFKQHNLS NGKNKLVELK NMPKDLSEKI DNNNKLMDKY GFYATPAMIW KDAKGEIQSQ
QGAPKDINKL LND
//
