PRSA_STRPS
ID PRSA_STRPS Reviewed; 313 AA.
AC B2IPD4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=SPCG_0956;
OS Streptococcus pneumoniae (strain CGSP14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=516950;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGSP14;
RX PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT "Genome evolution driven by host adaptations results in a more virulent and
RT antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL BMC Genomics 10:158-158(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; CP001033; ACB90208.1; -; Genomic_DNA.
DR RefSeq; WP_000727952.1; NC_010582.1.
DR AlphaFoldDB; B2IPD4; -.
DR SMR; B2IPD4; -.
DR EnsemblBacteria; ACB90208; ACB90208; SPCG_0956.
DR KEGG; spw:SPCG_0956; -.
DR HOGENOM; CLU_034646_6_0_9; -.
DR OMA; TMKGSTI; -.
DR Proteomes; UP000001682; 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..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT CHAIN 21..313
FT /note="Foldase protein PrsA"
FT /id="PRO_1000137387"
FT DOMAIN 143..241
FT /note="PpiC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
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 313 AA; 34413 MW; 42FEF736A40A8ED0 CRC64;
MKKKLLAGAI TLLSVATLAA CSKGSEGADL ISMKGDVITE HQFYEQVKSN PSAQQVLLNM
TIQKVFEKQY GSELDDKEVD DTIAEEKKQY GENYQRVLSQ AGMTLETRKA QIRTSKLVEL
AVKKVAEAEL TDEAYKKAFD EYTPDVTAQI IRLNNEDKAK EVLEKAKAEG ADFAQLAKDN
STDEKTKENG GEITFDSAST EVPEQVKKAA FALDVDGVSD VITATGTQAY SSQYYIVKLT
KKTEKSSNID DYKEKLKTVI LTQKQNDSTF VQSIIGKELQ AANIKVKDQA FQNIFTQYIG
GGDSSSSSST SNE