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 27-MAR-2024, entry version 133.
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; Bacillota; 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 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 KEGG; bar:GBAA_pXO2_0063; -.
DR PATRIC; fig|1392.230.peg.5911; -.
DR HOGENOM; CLU_014813_0_3_9; -.
DR OMA; ICGMGPP; -.
DR BioCyc; MetaCyc:GBAA_PXO2_0063-MONOMER; -.
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; 1.10.246.230; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR43199; GLUTATHIONE HYDROLASE; 1.
DR PANTHER; PTHR43199:SF1; GLUTATHIONE HYDROLASE PROENZYME; 1.
DR Pfam; PF01019; G_glu_transpept; 1.
DR PRINTS; PR01210; GGTRANSPTASE.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 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
//
