PRSA_GEOKA
ID PRSA_GEOKA Reviewed; 281 AA.
AC Q5L289;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=GK0656;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD74941.1; -; Genomic_DNA.
DR RefSeq; WP_011230159.1; NC_006510.1.
DR AlphaFoldDB; Q5L289; -.
DR SMR; Q5L289; -.
DR STRING; 235909.GK0656; -.
DR PRIDE; Q5L289; -.
DR EnsemblBacteria; BAD74941; BAD74941; GK0656.
DR KEGG; gka:GK0656; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_1_9; -.
DR OMA; TMKGSTI; -.
DR Proteomes; UP000001172; 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 GO; GO:0015031; P:protein transport; IEA:InterPro.
DR Gene3D; 1.10.3120.10; -; 1.
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; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR008880; Trigger_fac_C.
DR InterPro; IPR037041; Trigger_fac_C_sf.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR Pfam; PF05698; Trigger_C; 1.
DR SUPFAM; SSF109998; SSF109998; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 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;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT CHAIN 19..281
FT /note="Foldase protein PrsA"
FT /id="PRO_1000137383"
FT DOMAIN 133..223
FT /note="PpiC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
SQ SEQUENCE 281 AA; 31996 MW; 079A7575D11AE7AF CRC64;
MKKWMMAAAV VSLMALSACS NDGSEAIVET KNGNITKDEF YNEMKERVGK SVLRDLIDEK
VLSKKYKVTD EEIDREIERI KEAYGTQYDL AVQQNGEKVI REMVKLDLLR TKAAVEDIKV
TEKELKEYYD NYKPKIRASH ILVKDEKTAK EVKAKLDKGE DFSKLAKEYS QDPGSASNGG
DLGWFGPGKM VKEFEEAAYK LKVGEVSDPV KTDYGYHIIK VTDKEKKKSF NEMKDEIAFE
VKRNKLDPAT MQSKVDKLVK DAGVEIKDKD LQDVIEQQGK Q