ID   PRSA4_BACCR             Reviewed;         280 AA.
AC   Q81CB1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Foldase protein PrsA 4;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA4; OrderedLocusNames=BC_2862;
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; AAP09812.1; -; Genomic_DNA.
DR   RefSeq; NP_832611.1; NC_004722.1.
DR   RefSeq; WP_000823432.1; NZ_CP034551.1.
DR   PDB; 6VJ6; X-ray; 2.55 A; A/B=26-280.
DR   PDBsum; 6VJ6; -.
DR   AlphaFoldDB; Q81CB1; -.
DR   SMR; Q81CB1; -.
DR   STRING; 226900.BC_2862; -.
DR   EnsemblBacteria; AAP09812; AAP09812; BC_2862.
DR   KEGG; bce:BC2862; -.
DR   PATRIC; fig|226900.8.peg.2924; -.
DR   HOGENOM; CLU_034646_6_1_9; -.
DR   OMA; SEFGPGM; -.
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   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..280
FT                   /note="Foldase protein PrsA 4"
FT                   /id="PRO_0000029297"
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"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           38..66
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           71..85
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           89..92
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           93..96
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           101..119
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           124..128
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   STRAND          135..144
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           145..156
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           161..168
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   TURN            172..174
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           191..198
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   STRAND          214..223
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           229..246
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           248..260
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           269..274
FT                   /evidence="ECO:0007829|PDB:6VJ6"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:6VJ6"
SQ   SEQUENCE   280 AA;  32043 MW;  8EC0148F4FA911F0 CRC64;
     MKRKKLVIGS ILMGMTLSLS ACGSSDNIVT TKSGSISESD FNKKLKENYG KQNLSEMVVE
     KVLHDKYKVT DEEVTKQLEE LKDKMGDNFN TYMESNGVKN EDQLKEKLKL TFAFEKAIKA
     TVTEKDIKDH YKPKLQVSHI LVKDEKTAKE IKEKLNSGED FAALAKQYSE DPGSKEKGGE
     LSEFGPGMMV KEFEDAAYKL EVGQLSEPVK SSFGYHIIKL TDKKELKPYE EEKENIRKEL
     EQQRIQDPQF HQQVTRDLLK NADIKVSDKD LKDTFKELEK