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CAPD_BACAN
ID   CAPD_BACAN              Reviewed;         528 AA.
AC   Q51693; Q6F034; Q8KYD9; Q9RMX7;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Capsule biosynthesis protein CapD proenzyme;
DE            EC=2.3.2.-;
DE   Contains:
DE     RecName: Full=Capsule biosynthesis protein CapD large chain;
DE   Contains:
DE     RecName: Full=Capsule biosynthesis protein CapD small chain;
DE   Flags: Precursor;
GN   Name=capD; Synonyms=dep;
GN   OrderedLocusNames=pXO2-55, BXB0063, GBAA_pXO2_0063;
OS   Bacillus anthracis.
OG   Plasmid pXO2, and Plasmid pTE702.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Davis; PLASMID=pTE702;
RX   PubMed=8105361; DOI=10.1111/j.1365-2958.1993.tb01710.x;
RA   Uchida I., Makino S., Sasakawa C., Yoshikawa M., Sugimoto C., Terakado N.;
RT   "Identification of a novel gene, dep, associated with depolymerization of
RT   the capsular polymer in Bacillus anthracis.";
RL   Mol. Microbiol. 9:487-496(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Pasteur; PLASMID=pXO2;
RX   PubMed=10475962; DOI=10.1046/j.1365-2672.1999.00883.x;
RA   Okinaka R.T., Cloud K., Hampton O., Hoffmaster A., Hill K.K., Keim P.,
RA   Koehler T., Lamke G., Kumano S., Manter D., Martinez Y., Ricke D.,
RA   Svensson R., Jackson P.J.;
RT   "Sequence, assembly and analysis of pXO1 and pXO2.";
RL   J. Appl. Microbiol. 87:261-262(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ames / isolate Florida / A2012; PLASMID=pXO2;
RX   PubMed=12004073; DOI=10.1126/science.1071837;
RA   Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L.,
RA   Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D., Keim P.,
RA   Fraser C.M.;
RT   "Comparative genome sequencing for discovery of novel polymorphisms in
RT   Bacillus anthracis.";
RL   Science 296:2028-2033(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor; PLASMID=pXO2;
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   [5]
RP   FUNCTION.
RX   PubMed=12134259; DOI=10.1086/341299;
RA   Makino S., Watarai M., Cheun H.-I., Shirahata T., Uchida I.;
RT   "Effect of the lower molecular capsule released from the cell surface of
RT   Bacillus anthracis on the pathogenesis of anthrax.";
RL   J. Infect. Dis. 186:227-233(2002).
RN   [6]
RP   INDUCTION.
RC   PLASMID=pXO2;
RX   PubMed=14702298; DOI=10.1128/jb.186.2.307-315.2004;
RA   Drysdale M., Bourgogne A., Hilsenbeck S.G., Koehler T.M.;
RT   "atxA controls Bacillus anthracis capsule synthesis via acpA and a newly
RT   discovered regulator, acpB.";
RL   J. Bacteriol. 186:307-315(2004).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX   PubMed=19017271; DOI=10.1111/j.1365-2958.2008.06533.x;
RA   Richter S., Anderson V.J., Garufi G., Lu L., Budzik J.M., Joachimiak A.,
RA   He C., Schneewind O., Missiakas D.;
RT   "Capsule anchoring in Bacillus anthracis occurs by a transpeptidation
RT   reaction that is inhibited by capsidin.";
RL   Mol. Microbiol. 71:404-420(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 29-528 IN COMPLEX WITH
RP   GLUTAMYLGLUTAMATE, PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY,
RP   ACTIVE SITE, SUBUNIT, MUTAGENESIS OF THR-368; THR-370; SER-372 AND ARG-520,
RP   AND AUTOCATALYTIC CLEAVAGE.
RX   PubMed=19535342; DOI=10.1074/jbc.m109.019034;
RA   Wu R., Richter S., Zhang R.G., Anderson V.J., Missiakas D., Joachimiak A.;
RT   "Crystal structure of Bacillus anthracis transpeptidase enzyme CapD.";
RL   J. Biol. Chem. 284:24406-24414(2009).
CC   -!- FUNCTION: Transpeptidase that cleaves the poly-gamma-D-glutamate
CC       capsule and catalyzes the formation of an amide bond with the side-
CC       chain amino group of meso-diaminopimelic acid (m-DAP) in the
CC       peptidoglycan scaffold (PubMed:19017271). Degradation of the high-
CC       molecular weight capsule (H-capsule) to the lower-molecular weight
CC       capsule (L-capsule), which is released from the bacterial cell surface.
CC       The production of L-capsule is essential to mediate escape from host
CC       defenses. {ECO:0000269|PubMed:12134259, ECO:0000269|PubMed:19017271,
CC       ECO:0000269|PubMed:19535342, ECO:0000269|PubMed:8105361}.
CC   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC   -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are
CC       synthesized in precursor form from a single polypeptide.
CC       {ECO:0000269|PubMed:19535342}.
CC   -!- INDUCTION: Capsule synthesis is transcriptionally regulated by AtxA,
CC       AcpA and AcpB. {ECO:0000269|PubMed:14702298}.
CC   -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF13660.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA03126.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D14037; BAA03126.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF188935; AAF13660.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE011191; AAM26219.1; -; Genomic_DNA.
DR   EMBL; AE017335; AAT28993.2; -; Genomic_DNA.
DR   PIR; S36209; S36209.
DR   RefSeq; NP_053210.1; NC_002146.1.
DR   RefSeq; WP_010891443.1; NC_002146.1.
DR   PDB; 3G9K; X-ray; 1.79 A; D/L=29-351, F/S=352-528.
DR   PDB; 3GA9; X-ray; 2.30 A; L=29-351, S=352-528.
DR   PDBsum; 3G9K; -.
DR   PDBsum; 3GA9; -.
DR   AlphaFoldDB; Q51693; -.
DR   SMR; Q51693; -.
DR   MEROPS; T03.023; -.
DR   EnsemblBacteria; AAT28993; AAT28993; GBAA_pXO2_0063.
DR   KEGG; bar:GBAA_pXO2_0063; -.
DR   PATRIC; fig|1392.230.peg.5911; -.
DR   HOGENOM; CLU_014813_0_3_9; -.
DR   OMA; VCGMGPP; -.
DR   BRENDA; 3.4.19.13; 634.
DR   UniPathway; UPA00934; -.
DR   EvolutionaryTrace; Q51693; -.
DR   PRO; PR:Q51693; -.
DR   Proteomes; UP000000594; Plasmid pXO2.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.20.40; -; 1.
DR   InterPro; IPR043137; GGT_ssub.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   SUPFAM; SSF56235; SSF56235; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsule biogenesis/degradation; Direct protein sequencing;
KW   Hydrolase; Plasmid; Protease; Reference proteome; Signal; Transferase;
KW   Virulence; Zymogen.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..528
FT                   /note="Capsule biosynthesis protein CapD large chain"
FT                   /id="PRO_0000205980"
FT   CHAIN           352..528
FT                   /note="Capsule biosynthesis protein CapD small chain"
FT                   /id="PRO_0000424555"
FT   ACT_SITE        352
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:19017271,
FT                   ECO:0000269|PubMed:19535342"
FT   BINDING         352
FT                   /ligand="poly-gamma-D-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:189702"
FT                   /evidence="ECO:0000305|PubMed:19535342,
FT                   ECO:0007744|PDB:3G9K, ECO:0007744|PDB:3GA9"
FT   BINDING         429..432
FT                   /ligand="poly-gamma-D-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:189702"
FT                   /evidence="ECO:0000305|PubMed:19535342,
FT                   ECO:0007744|PDB:3G9K, ECO:0007744|PDB:3GA9"
FT   BINDING         520
FT                   /ligand="poly-gamma-D-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:189702"
FT                   /evidence="ECO:0000305|PubMed:19535342,
FT                   ECO:0007744|PDB:3G9K, ECO:0007744|PDB:3GA9"
FT   VARIANT         400
FT                   /note="S -> N (in strain: Pasteur)"
FT   MUTAGEN         368
FT                   /note="T->A: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:19535342"
FT   MUTAGEN         370
FT                   /note="T->A: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:19535342"
FT   MUTAGEN         372
FT                   /note="S->A: Slightly reduces enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:19535342"
FT   MUTAGEN         520
FT                   /note="R->A: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:19535342"
FT   STRAND          50..55
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           56..67
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           72..86
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   TURN            87..90
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          95..102
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           132..143
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           148..161
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           167..180
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:3GA9"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           190..192
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           204..216
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           219..222
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           224..234
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           238..242
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          247..249
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          252..256
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          259..263
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           270..282
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           285..288
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           292..312
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           324..327
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           330..334
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          353..358
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          364..370
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   TURN            374..377
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          414..418
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          421..426
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           430..432
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           433..445
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           451..456
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          460..463
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          466..471
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           475..482
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   TURN            483..485
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          487..490
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           494..497
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          501..506
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   TURN            507..510
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          511..515
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   HELIX           518..520
FT                   /evidence="ECO:0007829|PDB:3G9K"
FT   STRAND          523..526
FT                   /evidence="ECO:0007829|PDB:3G9K"
SQ   SEQUENCE   528 AA;  58084 MW;  5CC4CF263D650BF3 CRC64;
     MNSFKWGKKI ILFCLIVSLM GGIGVSCSFN KIKDSVKQKI DSMGDKGTYG VSASHPLAVE
     EGMKVLKNGG SAVDAAIVVS YVLGVVELHA SGIGGGGGML IISKDKETFI DYRETTPYFT
     GNQKPHIGVP GFVAGMEYIH DNYGSLPMGE LLQPAINYAE KGFKVDDSLT MRLDLAKPRI
     YSDKLSIFYP NGEPIETGET LIQTDLARTL KKIQKEGAKG FYEGGVARAI SKTAKISLED
     IKGYKVEVRK PVKGNYMGYD VYTAPPPFSG VTLLQMLKLA EKKEVYKDVD HTATYMSKME
     EISRIAYQDR KKNLGDPNYV NMDPNKMVSD KYISTMKNEN GDALSEAEHE STTHFVIIDR
     DGTVVSSTNT LSNFFGTGKY TAGFFLNNQL QNFGSEGFNS YEPGKRSRTF MAPTVLKKDG
     ETIGIGSPGG NRIPQILTPI LDKYTHGKGS LQDIINEYRF TFEKNTAYTE IQLSSEVKNE
     LSRKGLNVKK KVSPAFFGGV QALIKDERDN VITGAGDGRR NGTWKSNK
 
 
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