ID   PRSA2_BACCR             Reviewed;         285 AA.
AC   Q81GN0;
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 2;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA2; OrderedLocusNames=BC_1161;
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; AAP08148.1; -; Genomic_DNA.
DR   RefSeq; NP_830947.1; NC_004722.1.
DR   RefSeq; WP_001214214.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81GN0; -.
DR   SMR; Q81GN0; -.
DR   STRING; 226900.BC_1161; -.
DR   EnsemblBacteria; AAP08148; AAP08148; BC_1161.
DR   GeneID; 67505879; -.
DR   KEGG; bce:BC1161; -.
DR   PATRIC; fig|226900.8.peg.1125; -.
DR   HOGENOM; CLU_034646_6_1_9; -.
DR   OMA; QKAKNQY; -.
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   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; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..285
FT                   /note="Foldase protein PrsA 2"
FT                   /id="PRO_0000029295"
FT   DOMAIN          134..224
FT                   /note="PpiC"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   285 AA;  32235 MW;  E4C836CD3C8F0054 CRC64;
     MRGKHIFIIT ALISILMLSA CGQKNGSATV ATATDSTITK DNFEKQLKDR YGKDMLYEMM
     AQDVITKKYK VPDEEVNKEV EKVKKQYGDQ FKKVLENYGL KDEEDFKNQI KFKLAMNEAI
     KKSITEKDVK DHYKPEIKAS HILVSDENEA KEIKSKLDAG ASFEELAKQE SQDLLSKDKG
     GDLGYFNSGT MAPEFETAAY KLNVGQISNP VKSSNGYHVI KLTDKKALKP YDEVKDSIRK
     NLEEERTADP VFSKKLLQEE LKKANIKIND SDLKDTFTLV SPQGN