PRSA2_STRP3
ID PRSA2_STRP3 Reviewed; 309 AA.
AC P0DD44; Q8K5P3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Foldase protein PrsA 2;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA2; OrderedLocusNames=SpyM3_1740;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=198466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=12122206; DOI=10.1073/pnas.152298499;
RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT encoded toxins, the high-virulence phenotype, and clone emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
CC -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC translocational extracellular folding of several secreted proteins.
CC {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000305}.
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DR EMBL; AE014074; AAM80347.1; -; Genomic_DNA.
DR RefSeq; WP_002993567.1; NC_004070.1.
DR AlphaFoldDB; P0DD44; -.
DR SMR; P0DD44; -.
DR EnsemblBacteria; AAM80347; AAM80347; SpyM3_1740.
DR KEGG; spg:SpyM3_1740; -.
DR HOGENOM; CLU_034646_6_0_9; -.
DR OMA; SEFGPGM; -.
DR Proteomes; UP000000564; 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"
FT CHAIN 23..309
FT /note="Foldase protein PrsA 2"
FT /id="PRO_0000029332"
FT DOMAIN 146..241
FT /note="PpiC"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 309 AA; 34361 MW; 38DA7FFB2B1A02E8 CRC64;
MKQMNKLITG VVTLATVVTL SACQSSHNNT KLVSMKGDTI TVSDFYNETK NTELAQKAML
SLVISRVFET QYANKVSDKE VEKAYKQTAD QYGTSFKTVL AQSGLTPETY KKQIRLTKLV
EYAVKEQAKN ETISKKDYRQ AYDAYTPTMT AEIMQFEKEE DAKAALEAVK AEGADFAAIA
KEKTIAADKK TTYTFDSGET TLPAEVVRAA SGLKEGNRSE IITALDPATS KRTYHIIKVT
KKATKKADWK AYQKRLKDII VTGKLKDPDF QNKVIAKALD KANVKIKDKA FANILAQFAK
PNQKQPAQK