PRSA_CLOPS
ID PRSA_CLOPS Reviewed; 342 AA.
AC Q0SQ68;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Foldase protein PrsA {ECO:0000255|HAMAP-Rule:MF_01145};
DE EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_01145};
DE Flags: Precursor;
GN Name=prsA {ECO:0000255|HAMAP-Rule:MF_01145}; OrderedLocusNames=CPR_2492;
OS Clostridium perfringens (strain SM101 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=289380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM101 / Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
CC -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC translocational extracellular folding of several secreted proteins.
CC {ECO:0000255|HAMAP-Rule:MF_01145}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01145};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01145};
CC Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01145}.
CC -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000255|HAMAP-
CC Rule:MF_01145}.
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DR EMBL; CP000312; ABG87706.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0SQ68; -.
DR SMR; Q0SQ68; -.
DR EnsemblBacteria; ABG87706; ABG87706; CPR_2492.
DR KEGG; cpr:CPR_2492; -.
DR OMA; VESRNEP; -.
DR Proteomes; UP000001824; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.50.40; -; 1.
DR HAMAP; MF_01145; Foldase_PrsA; 1.
DR InterPro; IPR023059; Foldase_PrsA.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR Pfam; PF13145; Rotamase_2; 1.
DR SUPFAM; SSF109998; SSF109998; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Isomerase; Lipoprotein; Membrane; Palmitate; Rotamase;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT CHAIN 23..342
FT /note="Foldase protein PrsA"
FT /id="PRO_1000085051"
FT DOMAIN 190..284
FT /note="PpiC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
SQ SEQUENCE 342 AA; 38782 MW; 31543FC80BEA59C8 CRC64;
MVSVKKIVAS ALVGVLMFSA VGCNMVEKTQ AAIDKTTVAT VNGEKITLGE VDSHLKGVFT
QMKSQYGDKY MDDPQVAQQI LQQRQGILNS LVEEKILVVE ANKENIVPSE EELNKKIEQQ
IKLYKEQYGE EGYKKAVESM GYNEDTFKEY LKNQFIADAA ASNASKDIKV TDEEAQKYYD
ENKKQFEVQA KGVLARHLLF ENEEEAQKAY DEIQSGKTTF NDLFTKYENN KLEKKTPIAE
SFVVPDENAQ VAKEFVEGLK SLKEGEISKP IKTQFGYHII QAGATYEKGA QLPFNEVKSQ
IIQILKQQKD SQKLKSDMDQ WKKDLNVKVY DDKLQEGLKI SK