ID   PRSA_CLOAB              Reviewed;         333 AA.
AC   Q97E99;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   25-MAY-2022, entry version 97.
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=CA_C3215;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK81151.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE001437; AAK81151.1; ALT_INIT; Genomic_DNA.
DR   PIR; D97295; D97295.
DR   RefSeq; NP_349811.1; NC_003030.1.
DR   AlphaFoldDB; Q97E99; -.
DR   SMR; Q97E99; -.
DR   STRING; 272562.CA_C3215; -.
DR   EnsemblBacteria; AAK81151; AAK81151; CA_C3215.
DR   KEGG; cac:CA_C3215; -.
DR   PATRIC; fig|272562.8.peg.3394; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_5_2_9; -.
DR   OMA; QVRANMG; -.
DR   OrthoDB; 1838755at2; -.
DR   Proteomes; UP000000814; 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; IPR023058; PPIase_PpiC_CS.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   Pfam; PF13145; Rotamase_2; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 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..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   CHAIN           23..333
FT                   /note="Foldase protein PrsA"
FT                   /id="PRO_0000029300"
FT   DOMAIN          192..283
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   333 AA;  37622 MW;  BE10E12765DEDD94 CRC64;
     MKSAKQIATA LLVGMFTFSA VGCSMVEKRP EAINSKVVAT IYGNQTITRG EIDKLAKGTV
     EQLKSQYGDS YEKNEEAVAA LKKQKEQILT SLIDQKIFLK KAKDQKITLT KDEIKTNVDD
     VYAQYQQEFK TESEFKSQLS QYGYTVAEFK DQLKNRAISN KLIQQVVKDV KVSDDEAKKY
     YDSHKNSYTQ SPNTVHLAHI LVKTEKEAKA VKARIDKGED FATVAKQVST DGSKEKGGDL
     GDIQENDSNY DKTFMAAALK LNDNQVSAPV HTQFGWHVIK CIKKTEYPVK DFNSVKDDIK
     QTVLSTKQKS VYQKTLKKWE SQANIDKNEK NLM