ID   PRSA2_LACPL             Reviewed;         309 AA.
AC   Q88T16; F9UTA2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Foldase protein PrsA 2;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA2; Synonyms=prtM2; OrderedLocusNames=lp_3193;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
CC   -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC       translocational extracellular folding of several secreted proteins.
CC       {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: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000305}.
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DR   EMBL; AL935263; CCC80220.1; -; Genomic_DNA.
DR   RefSeq; WP_011102074.1; NC_004567.2.
DR   RefSeq; YP_004890734.1; NC_004567.2.
DR   AlphaFoldDB; Q88T16; -.
DR   SMR; Q88T16; -.
DR   STRING; 220668.lp_3193; -.
DR   DNASU; 1061958; -.
DR   EnsemblBacteria; CCC80220; CCC80220; lp_3193.
DR   KEGG; lpl:lp_3193; -.
DR   PATRIC; fig|220668.9.peg.2668; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_6_1_9; -.
DR   OMA; YHMILER; -.
DR   PhylomeDB; Q88T16; -.
DR   BioCyc; LPLA220668:G1GW0-2708-MON; -.
DR   Proteomes; UP000000432; 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   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;
KW   Reference proteome; Rotamase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..309
FT                   /note="Foldase protein PrsA 2"
FT                   /id="PRO_0000029308"
FT   DOMAIN          137..232
FT                   /note="PpiC"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   309 AA;  34308 MW;  C83BB1BF5CAEF8EB CRC64;
     MKYRLIGVGA SLVVAVMLTG CQAKATTLVK SDAGQVTQAE VFKQIENQAT TQQAVQELTL
     NKVLNQRYHV SQAEVTAKLK AFKRQAGANY HMILERNHVT EPRLKSQIKA NLLMEKAVSA
     KYPVTKAQLK KARAAYMPMT TVQHIATTNE KQAQKIIAEL NAGASFDSQV RKYQNNRQAH
     TTAGKLAQFD SYNQTLAPAI VQATAKLRVG HYVTKPVKTV MATADTKDKP TYEIINVVSR
     RSKTAAVTDD SGKQIDVTNY LREKIQQQRM MDKQTQVATI RSVFKAAHVK VVDAHFAPAF
     NDYLTTQNS