PPIC_SALTY
ID PPIC_SALTY Reviewed; 93 AA.
AC P0A265; Q9L6S3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase C;
DE Short=PPIase C;
DE EC=5.2.1.8;
DE AltName: Full=Parvulin;
DE AltName: Full=Rotamase C;
GN Name=ppiC; OrderedLocusNames=STM3910; ORFNames=STMD1.80;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It prefers amino
CC acid residues with hydrophobic side chains like leucine and
CC phenylalanine in the P1 position of the peptides substrates (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000305}.
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DR EMBL; AF233324; AAF33475.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22760.1; -; Genomic_DNA.
DR RefSeq; NP_462801.1; NC_003197.2.
DR RefSeq; WP_001096806.1; NC_003197.2.
DR AlphaFoldDB; P0A265; -.
DR SMR; P0A265; -.
DR STRING; 99287.STM3910; -.
DR PaxDb; P0A265; -.
DR EnsemblBacteria; AAL22760; AAL22760; STM3910.
DR GeneID; 1255436; -.
DR KEGG; stm:STM3910; -.
DR PATRIC; fig|99287.12.peg.4132; -.
DR HOGENOM; CLU_090028_6_1_6; -.
DR OMA; GPVRTQF; -.
DR PhylomeDB; P0A265; -.
DR BioCyc; SENT99287:STM3910-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..93
FT /note="Peptidyl-prolyl cis-trans isomerase C"
FT /id="PRO_0000193419"
FT DOMAIN 2..91
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ SEQUENCE 93 AA; 10328 MW; DB929A1FF00EB0F0 CRC64;
MAKMAAALHI LVKEEKLALD LLEQIKNGGD FEKLAKKHSI CPSGKKGGHL GEFRQGQMVP
AFDKVVFSCP VLEPTGPLHT QFGYHIIKVL YRK
