PRSA1_BACCR
ID PRSA1_BACCR Reviewed; 286 AA.
AC Q81GY5;
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 1;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA1; OrderedLocusNames=BC_1043;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP08030.1; -; Genomic_DNA.
DR RefSeq; NP_830829.1; NC_004722.1.
DR RefSeq; WP_000710058.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81GY5; -.
DR SMR; Q81GY5; -.
DR STRING; 226900.BC_1043; -.
DR MetOSite; Q81GY5; -.
DR EnsemblBacteria; AAP08030; AAP08030; BC_1043.
DR GeneID; 67505761; -.
DR KEGG; bce:BC1043; -.
DR PATRIC; fig|226900.8.peg.1001; -.
DR HOGENOM; CLU_034646_6_1_9; -.
DR OMA; TMKGSTI; -.
DR Proteomes; UP000001417; 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; IPR037041; Trigger_fac_C_sf.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
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"
FT CHAIN 19..286
FT /note="Foldase protein PrsA 1"
FT /id="PRO_0000029294"
FT DOMAIN 130..220
FT /note="PpiC"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 286 AA; 32424 MW; 5F2A080EEE15AE94 CRC64;
MKKAMLALAA TSVIALSACG TSSSDKIVTS KAGDITKEEF YDQMKTQAGK QVLNNMVMEK
VLIKNYKVED KDVDKKFDEM KKQYGDQFDT LLKQQGIKEE TIKTGVRAQL AQEKAIEKTI
TDKELKENYK PEIKASHILV KDEATAKKVK EELGQGKSFE ELAKQYSEDT GSKEKGGDLG
YFTAGKMVKE FEDAAYKLKK DEVSEPVKSQ FGYHIIKVTD IKEQKPFDEV KGDIKKDLVQ
KKAQDAAFMN DLMMKEIKKA DVKVDDKDLK DLFEEKKADD KKEEKK