PRSA1_STRP3
ID PRSA1_STRP3 Reviewed; 351 AA.
AC P0DD42; P60751; Q99Z56;
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 1;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA1; OrderedLocusNames=SpyM3_1059;
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; AAM79666.1; -; Genomic_DNA.
DR RefSeq; WP_002984003.1; NC_004070.1.
DR AlphaFoldDB; P0DD42; -.
DR SMR; P0DD42; -.
DR EnsemblBacteria; AAM79666; AAM79666; SpyM3_1059.
DR KEGG; spg:SpyM3_1059; -.
DR HOGENOM; CLU_034646_6_0_9; -.
DR OMA; TMKGSTI; -.
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..351
FT /note="Foldase protein PrsA 1"
FT /id="PRO_0000029331"
FT DOMAIN 145..240
FT /note="PpiC"
FT REGION 303..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 351 AA; 38535 MW; EE3A620A26EEF3A8 CRC64;
MKNSNKLIAS VVTLASVMAL AACQSTNDNT KVISMKGDTI SVSDFYNETK NTEVSQKAML
NLVISRVFEA QYGDKVSKKE VEKAYHKTAE QYGASFSAAL AQSSLTPETF KRQIRSSKLV
EYAVKEAAKK ELTTQEYKKA YESYTPTMAV EMITLDNEET AKSVLEELKA EGADFTAIAK
EKTTTPEKKV TYKFDSGATN VPTDVVKAAS SLNEGGISDV ISVLDPTSYQ KKFYIVKVTK
KAEKKSDWQE YKKRLKAIII AEKSKDMNFQ NKVIANALDK ANVKIKDKAF ANILAQYANL
GQKTKAASES STTSESSKAA EENPSESEQT QTSSAEEPTE TEAQTQEPAA Q