PRSA_STRPI
ID PRSA_STRPI Reviewed; 313 AA.
AC B1IBE1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=SPH_1082;
OS Streptococcus pneumoniae (strain Hungary19A-6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=487214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hungary19A-6;
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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; CP000936; ACA37287.1; -; Genomic_DNA.
DR RefSeq; WP_000727935.1; NC_010380.1.
DR PDB; 5TVL; X-ray; 2.55 A; A/B/C/D=27-313.
DR PDBsum; 5TVL; -.
DR AlphaFoldDB; B1IBE1; -.
DR SMR; B1IBE1; -.
DR EnsemblBacteria; ACA37287; ACA37287; SPH_1082.
DR GeneID; 60234013; -.
DR GeneID; 66806104; -.
DR KEGG; spv:SPH_1082; -.
DR HOGENOM; CLU_034646_6_0_9; -.
DR OMA; TMKGSTI; -.
DR Proteomes; UP000002163; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Isomerase; Lipoprotein; Membrane; Palmitate;
KW Rotamase; 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_1000137386"
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"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:5TVL"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 51..70
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 105..128
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:5TVL"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:5TVL"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:5TVL"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:5TVL"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:5TVL"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:5TVL"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5TVL"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5TVL"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:5TVL"
SQ SEQUENCE 313 AA; 34440 MW; 44063A36ABF9BED0 CRC64;
MKKKLLAGAI TLLSVATLAA CSKGSEGADL ISMKGDVITE HQFYEQVKNN 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
