ID   PRSA2_STRP6             Reviewed;         309 AA.
AC   Q5X9P6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Foldase protein PrsA 2 {ECO:0000255|HAMAP-Rule:MF_01145};
DE            EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_01145};
DE   Flags: Precursor;
GN   Name=prsA2 {ECO:0000255|HAMAP-Rule:MF_01145}; OrderedLocusNames=M6_Spy1732;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
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; CP000003; AAT87867.1; -; Genomic_DNA.
DR   RefSeq; WP_011889195.1; NC_006086.1.
DR   AlphaFoldDB; Q5X9P6; -.
DR   SMR; Q5X9P6; -.
DR   PRIDE; Q5X9P6; -.
DR   EnsemblBacteria; AAT87867; AAT87867; M6_Spy1732.
DR   KEGG; spa:M6_Spy1732; -.
DR   HOGENOM; CLU_034646_6_0_9; -.
DR   Proteomes; UP000001167; 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; Rotamase;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   CHAIN           23..309
FT                   /note="Foldase protein PrsA 2"
FT                   /id="PRO_0000029334"
FT   DOMAIN          146..241
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   309 AA;  34374 MW;  2D1595DEE4F032E8 CRC64;
     MKQMNKLITG VVTLATVVTL SACQSSHNNT KLVSMKGDTI TVSDFYNETK NTELAQKAML
     SLVISRVFET QYANKVSDKE VEKAYKQTAD QYGTSFKTVL AQSGLTPETY KKQIRLTKLV
     EYAVKEQAKN ETISKKDYRQ AYDAYTPTMT AEIMQFEKEE DAKAALEAVK AEGADFAAIA
     KEKTIAADKK TTYTFDSGET TLPAEVVRAA SGLKEGNRSE IITALDPAIS KRTYHIIKVT
     KKATKKADWK AYQKRLKDII VTGKLKDPDF QNKVIAKALD KANVKIKDKA FANILAQFAK
     PNQKQPAQK