PRSA_STRE4
ID PRSA_STRE4 Reviewed; 333 AA.
AC C0M9L5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=SEQ_0694;
OS Streptococcus equi subsp. equi (strain 4047).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4047;
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204883; CAW93050.1; -; Genomic_DNA.
DR RefSeq; WP_012679220.1; NC_012471.1.
DR AlphaFoldDB; C0M9L5; -.
DR SMR; C0M9L5; -.
DR PRIDE; C0M9L5; -.
DR EnsemblBacteria; CAW93050; CAW93050; SEQ_0694.
DR KEGG; seu:SEQ_0694; -.
DR HOGENOM; CLU_034646_6_0_9; -.
DR OMA; TMKGSTI; -.
DR OrthoDB; 1838755at2; -.
DR Proteomes; UP000001365; 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..333
FT /note="Foldase protein PrsA"
FT /id="PRO_5000453274"
FT DOMAIN 145..240
FT /note="PpiC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT REGION 301..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 36562 MW; 400FA76118B30A1D CRC64;
MKKSTKLLAG IVTLASAMTL AACQSTNDNT SVITMKGDTI SVSDFYNETK NTEISQRAML
NLVVSRVFED QYGKKVSKKR TEEAYNKSAE QYGASFSAAL AQSGLTTDTY KRQIRSAMLV
EYAVKEAAKK ELTDADYKKA YESYTPEMTT QVTTLDNEET AKAVLGEVKA EGADFAAIAK
EKTTAADKKV DYKFDSGDTK LPADVIKAAS GLKEGDISEV VSVLDPATYQ NKFYIVKVTK
KAEKASDWKK YKKRLKEIVL AEKTQNIDFQ NKVIAKALDK ANVKIKDQAF ANILAQYANT
DKKASKANTS KSDQKSSSDS SKDSQSSKSK SEK