ID   PRSA3_BACCR             Reviewed;         283 AA.
AC   Q81DT1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Foldase protein PrsA 3;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA3; OrderedLocusNames=BC_2272;
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; AAP09236.1; -; Genomic_DNA.
DR   RefSeq; NP_832035.1; NC_004722.1.
DR   RefSeq; WP_000727349.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81DT1; -.
DR   SMR; Q81DT1; -.
DR   STRING; 226900.BC_2272; -.
DR   EnsemblBacteria; AAP09236; AAP09236; BC_2272.
DR   KEGG; bce:BC2272; -.
DR   PATRIC; fig|226900.8.peg.2295; -.
DR   HOGENOM; CLU_034646_6_1_9; -.
DR   OMA; VESRNEP; -.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..283
FT                   /note="Foldase protein PrsA 3"
FT                   /id="PRO_0000029296"
FT   DOMAIN          132..222
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"
SQ   SEQUENCE   283 AA;  32144 MW;  3B048A4F62DE00CE CRC64;
     MKKKKIFIGT IISCVMLALS ACGSSDNVVT SKVGNVTEKE LSKELRQQYG ESTLYQMMLS
     KALLDKYKVS DEEAKKKVEE AKDKMGENFK STLEQLGLKN EDELKEKMKP EIAFEKAIKA
     TVTDKDVKNN YKPEMKVSHI LVKDEKTAKE IKEKVNNGED FAALANQYSE DTGSKEQGGE
     ISGFAPGQTV KEFEEAAYKL DAGQVSDPVK TTYGYHIIKV TDKKELKPFD EVKDKIRKDI
     EQQRLQDTTG KWKQQVVNDL LKDADIKVNN KEFKDTFKFL EKK