ID   PRSA_LIGS1              Reviewed;         296 AA.
AC   Q1WUQ1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=LSL_0475;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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; CP000233; ABD99284.1; -; Genomic_DNA.
DR   RefSeq; WP_003699757.1; NC_007929.1.
DR   RefSeq; YP_535367.1; NC_007929.1.
DR   AlphaFoldDB; Q1WUQ1; -.
DR   SMR; Q1WUQ1; -.
DR   STRING; 362948.LSL_0475; -.
DR   DNASU; 3976851; -.
DR   EnsemblBacteria; ABD99284; ABD99284; LSL_0475.
DR   KEGG; lsl:LSL_0475; -.
DR   PATRIC; fig|362948.14.peg.551; -.
DR   HOGENOM; CLU_034646_6_1_9; -.
DR   OMA; SEFGPGM; -.
DR   Proteomes; UP000006559; 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|HAMAP-Rule:MF_01145"
FT   CHAIN           21..296
FT                   /note="Foldase protein PrsA"
FT                   /id="PRO_1000164113"
FT   DOMAIN          136..232
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
SQ   SEQUENCE   296 AA;  32748 MW;  0B02E03698B6D507 CRC64;
     MKKKWLVAIS GIVLTFGLAA CSKTVATTSG GKITESEYYS SMKKTSSGKQ VLQQMILNKV
     LEKEYGSKVS DKKVNEQYNT YKKQYGSSFD SVLAQNDMTK SSFKQEIRSN LLLKEAVKDN
     TKITNKQLKA QWKEYEPKVT VAHILVSKKS TAEDIINKLK EDGSYANFKK LAKKYSTDSS
     TKNDGGKLAA FDNTDTSLDS TFKKAAFGLK QGSFTTEPVK TEYGYHVIYS IKNPGKGKMS
     DHTSELKSQI IDSKMSDSTT LQTVVSKVLK KGNVSIKDKD LQNILSSYLG SSSSSK