PRSA3_BACAN
ID PRSA3_BACAN Reviewed; 283 AA.
AC Q81QT1; Q6HYZ9; Q6KSZ8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Foldase protein PrsA 3;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA3; Synonyms=prsA-3; OrderedLocusNames=BA_2336, GBAA_2336, BAS2178;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP CHARACTERIZATION.
RX PubMed=12606539; DOI=10.1074/jbc.m301244200;
RA Williams R.C., Rees M.L., Jacobs M.F., Pragai Z., Thwaite J.E.,
RA Baillie L.W., Emmerson P.T., Harwood C.R.;
RT "Production of Bacillus anthracis protective antigen is dependent on the
RT extracellular chaperone, PrsA.";
RL J. Biol. Chem. 278:18056-18062(2003).
CC -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC translocational extracellular folding of several secreted proteins.
CC Important for the secretion of the protective antigen. The three PsrA
CC proteins in this organism show different but overlapping substrate
CC specificities.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP26206.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAT31456.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016879; AAP26206.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017334; AAT31456.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE017225; AAT54490.1; -; Genomic_DNA.
DR RefSeq; NP_844720.1; NC_003997.3.
DR RefSeq; WP_000727474.1; NZ_WXXI01000004.1.
DR RefSeq; YP_028439.1; NC_005945.1.
DR AlphaFoldDB; Q81QT1; -.
DR SMR; Q81QT1; -.
DR STRING; 260799.BAS2178; -.
DR PRIDE; Q81QT1; -.
DR DNASU; 1084443; -.
DR EnsemblBacteria; AAP26206; AAP26206; BA_2336.
DR EnsemblBacteria; AAT31456; AAT31456; GBAA_2336.
DR GeneID; 45022219; -.
DR KEGG; ban:BA_2336; -.
DR KEGG; bar:GBAA_2336; -.
DR KEGG; bat:BAS2178; -.
DR PATRIC; fig|198094.11.peg.2305; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_1_9; -.
DR OMA; VESRNEP; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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 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_0000029293"
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; 32083 MW; C980025975B983CB CRC64;
MKKKKLFLGT IISCVVLALS ACGSSDNVVT SKVGNITEKE LSKELRQKYG ESTLYQMVLS
KALLDKYKVS DEEAKKQVEE AKDKMGDNFK STLEQVGLKN EDELKEKMKP EIAFEKAIKA
TVTEKDVKDN YKPEMKVSHI LVKDEKTAKE VKEKVNNGED FAALAKQYSE DTGSKEQGGE
ITGFAPGQTV KEFEEAAYKL DAGQVSEPVK TTYGYHIIKV TDKKELKPFD EVKDSIRKDI
EQQRLQDTTG KWKQQVVNEL LKDADIKVND KEFKNTFEFL EKK
