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PRSA2_BACAN
ID   PRSA2_BACAN             Reviewed;         285 AA.
AC   Q81TU1; Q6I224; Q6KVW2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Foldase protein PrsA 2;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA2; Synonyms=prsA-2; OrderedLocusNames=BA_1169, GBAA_1169, BAS1084;
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}.
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DR   EMBL; AE016879; AAP25134.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT30258.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT53407.1; -; Genomic_DNA.
DR   RefSeq; NP_843648.1; NC_003997.3.
DR   RefSeq; WP_001214195.1; NZ_WXXJ01000044.1.
DR   RefSeq; YP_027356.1; NC_005945.1.
DR   PDB; 6VJ4; X-ray; 1.70 A; A=29-285.
DR   PDBsum; 6VJ4; -.
DR   AlphaFoldDB; Q81TU1; -.
DR   SMR; Q81TU1; -.
DR   STRING; 261594.GBAA_1169; -.
DR   DNASU; 1089182; -.
DR   EnsemblBacteria; AAP25134; AAP25134; BA_1169.
DR   EnsemblBacteria; AAT30258; AAT30258; GBAA_1169.
DR   GeneID; 45021180; -.
DR   KEGG; ban:BA_1169; -.
DR   KEGG; bar:GBAA_1169; -.
DR   KEGG; bat:BAS1084; -.
DR   PATRIC; fig|198094.11.peg.1148; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_6_1_9; -.
DR   OMA; QKAKNQY; -.
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; IPR023058; PPIase_PpiC_CS.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   Pfam; PF00639; Rotamase; 1.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..285
FT                   /note="Foldase protein PrsA 2"
FT                   /id="PRO_0000029292"
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"
FT   HELIX           55..68
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           73..87
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           91..97
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           103..122
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           126..131
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   STRAND          137..145
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           147..158
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           163..170
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           174..177
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   TURN            178..181
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   STRAND          182..186
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           193..201
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   STRAND          216..225
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           231..247
FT                   /evidence="ECO:0007829|PDB:6VJ4"
FT   HELIX           250..263
FT                   /evidence="ECO:0007829|PDB:6VJ4"
SQ   SEQUENCE   285 AA;  32079 MW;  D328DD7C3B6CAB5B CRC64;
     MRGKHIFIIT ALISILMLAA CGQKNSSATV ATATDSTITK SDFEKQLKDR YGKDMLYEMI
     AQDVITKKYK VSDDDVDKEV QKAKSQYGDQ FKNVLKNNGL KDEADFKNQI KFKLSMNKAI
     KQSVTEKDVK DHYKPEIKAS HILVSDENEA KEIKKKLDTG ASFEELAKQE SQDLLSKEKG
     GDLGYFHSGA MTPEFETAAY KLKIGQISDP VQSPNGYHII KLTGKKDLKP YDEVKNSIRK
     NLEEERTADP IFGKKLLQSE LKKANIKIND SELEDTFTIV SPQGN
 
 
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