ID   PRSA_LATSS              Reviewed;         303 AA.
AC   Q38XZ9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=LCA_0626;
OS   Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS   subsp. sakei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Latilactobacillus.
OX   NCBI_TaxID=314315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23K;
RX   PubMed=16273110; DOI=10.1038/nbt1160;
RA   Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA   Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA   Zagorec M.;
RT   "The complete genome sequence of the meat-borne lactic acid bacterium
RT   Lactobacillus sakei 23K.";
RL   Nat. Biotechnol. 23:1527-1533(2005).
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; CR936503; CAI54930.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q38XZ9; -.
DR   SMR; Q38XZ9; -.
DR   STRING; 314315.LCA_0626; -.
DR   EnsemblBacteria; CAI54930; CAI54930; LCA_0626.
DR   KEGG; lsa:LCA_0626; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_6_1_9; -.
DR   OMA; SEFGPGM; -.
DR   Proteomes; UP000002707; 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..303
FT                   /note="Foldase protein PrsA"
FT                   /id="PRO_1000164114"
FT   DOMAIN          137..233
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   303 AA;  33560 MW;  925E858BCD097E36 CRC64;
     MMKKWLLAAA SLLMVVTLAG CGSNTIATLK GGKVTQDEFY KEIKETSAGK QQVQQMILQK
     ALQEQYGSKS LTKKIDKTYN TYKKQYGSSF TSVLAQSGLT TSSFKNQITT QMLANAALKA
     NKKVTNADLK KQWKTYEPKV EVQHILVEKK DTAETVISEL KKDNSTKNFT ALAKKYSTDT
     GTKKDGGKLP VFDSTDTSLD PTFKTAAFKL KTNEYTTTPV KTSYGYHVIR MIKNPGKGKM
     ADHKKTLTDQ VYAKWANDQT VMAKVYTKVL KKADVTIKDK DLSDILSSYG VNAKKSSAKS
     SSK