PRSA_CLOTE
ID PRSA_CLOTE Reviewed; 339 AA.
AC Q899I2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=CTC_00195;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO34844.1; -; Genomic_DNA.
DR RefSeq; WP_011098514.1; NC_004557.1.
DR AlphaFoldDB; Q899I2; -.
DR SMR; Q899I2; -.
DR STRING; 212717.CTC_00195; -.
DR EnsemblBacteria; AAO34844; AAO34844; CTC_00195.
DR GeneID; 64181035; -.
DR KEGG; ctc:CTC_00195; -.
DR HOGENOM; CLU_034646_5_2_9; -.
DR OMA; VESRNEP; -.
DR Proteomes; UP000001412; 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 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;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT CHAIN 27..339
FT /note="Foldase protein PrsA"
FT /id="PRO_0000029302"
FT DOMAIN 197..287
FT /note="PpiC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
SQ SEQUENCE 339 AA; 39021 MW; 11AD5FB61DF3DCA4 CRC64;
MKHLKNNTKK FTALLFALLF SMSIAGCNMI EKTPEAIEKS PVAKVGKKTI TRGELDTYPI
LAEQLTKLKE QFGGDLSKNA EIKDQLIQFK SQVLEQMIQE EIVFEKSEEL KVDNAKVEKE
VEKNLKNFMD QGFQGNKDKY KEDLKKMGTT EESIKRFFKA QVITEEVSKQ VVKDVKVDDN
TAKKHYEESK YTFTVNKPTF HAQHVLVKTE EEAKKVKARL DKGEDIKKIA KELSIDPSAK
ENSGDLGKAP YSSMVKPFAD AIVKLNKGEI SQPVKSQFGY HVIKLIDKDE VTFKDFNSVK
EQIKKDLLET EKRKVFNEKI EQWKKELKVE TKKYEKNII
