PRSA1_LISMO
ID PRSA1_LISMO Reviewed; 294 AA.
AC Q8Y759;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Foldase protein PrsA 1;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA1; OrderedLocusNames=lmo1444;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC translocational extracellular folding of several secreted proteins.
CC {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000305}.
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DR EMBL; AL591979; CAC99522.1; -; Genomic_DNA.
DR PIR; AD1255; AD1255.
DR RefSeq; NP_464969.1; NC_003210.1.
DR RefSeq; WP_003721949.1; NZ_CP023861.1.
DR PDB; 5HTF; X-ray; 2.10 A; A/B=22-294.
DR PDBsum; 5HTF; -.
DR AlphaFoldDB; Q8Y759; -.
DR SMR; Q8Y759; -.
DR STRING; 169963.lmo1444; -.
DR PaxDb; Q8Y759; -.
DR EnsemblBacteria; CAC99522; CAC99522; CAC99522.
DR GeneID; 986457; -.
DR KEGG; lmo:lmo1444; -.
DR PATRIC; fig|169963.11.peg.1483; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_1_9; -.
DR OMA; SEFGPGM; -.
DR PhylomeDB; Q8Y759; -.
DR BioCyc; LMON169963:LMO1444-MON; -.
DR Proteomes; UP000000817; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Isomerase; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..294
FT /note="Foldase protein PrsA 1"
FT /id="PRO_0000029313"
FT DOMAIN 135..226
FT /note="PpiC"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:5HTF"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 37..65
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 99..117
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:5HTF"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:5HTF"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:5HTF"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 251..265
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5HTF"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:5HTF"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5HTF"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:5HTF"
SQ SEQUENCE 294 AA; 32570 MW; 190C705A0BF31EB7 CRC64;
MTKLKKVMIS VIAATLLLLA GCGSSAVIKT DAGSVTQDEL YEAMKTTYGN EVVQQLTFKK
ILEDKYTVTE KEVNAEYKKY EEQYGDSFES TLSSNNLTKT SFKENLEYNL LVQKATEANM
DVSESKLKAY YKTWEPDITV RHILVDDEAT AKEIQTKLKN GEKFTDLAKE YSTDTATSTN
GGLLDPFGPG EMDETFEKAA YALENKDDVS GIVKSTYGYH LIQLVKKTEK GTYAKEKANV
KAAYIKSQLT SENMTAALKK ELKAANIDIK DSDLKDAFAD YTSTSSTSST TTSN
