ID   PRSA_STRSV              Reviewed;         335 AA.
AC   A3CLY1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=SSA_0753;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN44186.1; -; Genomic_DNA.
DR   RefSeq; WP_011836702.1; NC_009009.1.
DR   RefSeq; YP_001034736.1; NC_009009.1.
DR   AlphaFoldDB; A3CLY1; -.
DR   SMR; A3CLY1; -.
DR   STRING; 388919.SSA_0753; -.
DR   EnsemblBacteria; ABN44186; ABN44186; SSA_0753.
DR   KEGG; ssa:SSA_0753; -.
DR   PATRIC; fig|388919.9.peg.721; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_6_0_9; -.
DR   OMA; TMKGSTI; -.
DR   OrthoDB; 1838755at2; -.
DR   Proteomes; UP000002148; 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;
KW   Reference proteome; Rotamase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   CHAIN           21..335
FT                   /note="Foldase protein PrsA"
FT                   /id="PRO_1000085064"
FT   DOMAIN          142..239
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   REGION          300..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   335 AA;  36314 MW;  9823B10303485DB0 CRC64;
     MKKKIFAGAV TLLSVAVLAA CSNSEGKDIV TMKGNTITVN EFYDQVKNNG AAQQVLLQMA
     IKDIFEEKYG KDVKDKDVKD AFEKSKTAYG TAFAQVLAQN GLTEDAYKEQ IRTNMLVEYA
     VKKAAEKELT DENYKSAFEN YTPEVTAQII KVDSEDKGKE VLEKAKAEGA DFSQIAKENS
     TDAATKEKGG EIKFDSGSTD VPDAVKKAAF ALEENGVSDL VTVPDSQYSA SYYIVKLVKK
     SEKSSNWKDY KDKLKKIIIA QKEKDTSFIQ SVVAKELKDA NIKVKDSAFQ SVFAQYIETT
     GSSTSSSSAA SSSKTSESSS AAESSSKEAS SSAAE