DSBG_PSEAE
ID DSBG_PSEAE Reviewed; 256 AA.
AC Q9I106;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Thiol:disulfide interchange protein DsbG;
DE Flags: Precursor;
GN Name=dsbG; OrderedLocusNames=PA2476;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Involved in disulfide bond formation. Functions probably as a
CC disulfide isomerase with a narrower substrate specificity than DsbC.
CC DsbG is maintained in a reduced state by DsbD (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG05864.1; -; Genomic_DNA.
DR PIR; D83336; D83336.
DR RefSeq; NP_251166.1; NC_002516.2.
DR RefSeq; WP_003089790.1; NZ_QZGE01000008.1.
DR AlphaFoldDB; Q9I106; -.
DR SMR; Q9I106; -.
DR STRING; 287.DR97_5698; -.
DR PaxDb; Q9I106; -.
DR PRIDE; Q9I106; -.
DR EnsemblBacteria; AAG05864; AAG05864; PA2476.
DR GeneID; 882549; -.
DR KEGG; pae:PA2476; -.
DR PATRIC; fig|208964.12.peg.2587; -.
DR PseudoCAP; PA2476; -.
DR HOGENOM; CLU_080090_0_0_6; -.
DR InParanoid; Q9I106; -.
DR OMA; CPYCNMF; -.
DR PhylomeDB; Q9I106; -.
DR BioCyc; PAER208964:G1FZ6-2511-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR Gene3D; 3.10.450.70; -; 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 Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54423; SSF54423; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Periplasm; Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..256
FT /note="Thiol:disulfide interchange protein DsbG"
FT /id="PRO_0000034280"
FT DISULFID 134..137
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 256 AA; 28053 MW; C1EB26268781CE23 CRC64;
MRLPRNLITL GLGLTLLNAG LATAAEELPA PIRMVQEKGA RILGSFDAPD GLRGYAAEYQ
NQGMALYLTP DGKHVLTGHL FDAQGKDLSR EPLERLVYAP LAKEMWQKME QSAWIADGRA
DAPRVVYLFS DPNCPYCTMF WEQARPWVDA GKVQLRHIMV GIIREDSEAK SAALLASKDP
QKALHDHEQA GKASTLKPLA KIPAAVRKQL AGNMELMESM GAAATPAIFY LNAEGRMQQQ
QGAPQPDQLA EILGPR