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Database: UniProt/TrEMBL
Entry: C7BZC1_HELPB
LinkDB: C7BZC1_HELPB
Original site: C7BZC1_HELPB 
ID   C7BZC1_HELPB            Unreviewed;       349 AA.
AC   C7BZC1;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-SEP-2017, entry version 63.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754435};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754435};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
GN   Name=ddlA {ECO:0000313|EMBL:CAX29162.1};
GN   Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=HELPY_0629 {ECO:0000313|EMBL:CAX29162.1};
OS   Helicobacter pylori (strain B38).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=592205 {ECO:0000313|EMBL:CAX29162.1, ECO:0000313|Proteomes:UP000000313};
RN   [1] {ECO:0000313|EMBL:CAX29162.1, ECO:0000313|Proteomes:UP000000313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B38 {ECO:0000313|EMBL:CAX29162.1,
RC   ECO:0000313|Proteomes:UP000000313};
RX   PubMed=20537153; DOI=10.1186/1471-2164-11-368;
RA   Thiberge J.M., Boursaux-Eude C., Lehours P., Dillies M.A., Creno S.,
RA   Coppee J.Y., Rouy Z., Lajus A., Ma L., Burucoa C.,
RA   Ruskone-Foumestraux A., Courillon-Mallet A., De Reuse H., Boneca I.G.,
RA   Lamarque D., Megraud F., Delchier J.C., Medigue C., Bouchier C.,
RA   Labigne A., Raymond J.;
RT   "From array-based hybridization of Helicobacter pylori isolates to the
RT   complete genome sequence of an isolate associated with MALT
RT   lymphoma.";
RL   BMC Genomics 11:368-368(2010).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00754456}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00754451}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00754472};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00754454};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00644812}.
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DR   EMBL; FM991728; CAX29162.1; -; Genomic_DNA.
DR   ProteinModelPortal; C7BZC1; -.
DR   EnsemblBacteria; CAX29162; CAX29162; HELPY_0629.
DR   KEGG; hpb:HELPY_0629; -.
DR   HOGENOM; HOG000102494; -.
DR   KO; K01921; -.
DR   OMA; YDTKYIN; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000313; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR005905; D_ala_D_ala.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
DR   PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644673};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644718};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644792};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000313};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00754427};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:CAX29162.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00754439};
KW   Manganese {ECO:0000256|SAAS:SAAS00754447};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00754442};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644705};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644714}.
FT   DOMAIN      136    334       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   349 AA;  39864 MW;  636128C8EC4A4948 CRC64;
     MIVEFCVLFG GASFEHEISV VSAIALKGVL KDRIKYFIFL DENHHFYLIE ESNMHSKYFA
     QIKEKKLPPL ILTHNGLLKN SFLGTKIIEL PLVINLVHGG DGEDGKLASL LEFYRIAFIG
     PRIEASVLSY NKYLTKLYAK DLGVKTLDYA LLNEKNRANA LDLIGFNFPF IVKPSNAGSS
     LGVSVVKEEK ELIYALDSAF EYSKEVLIEP FIQGVKEYNL AGCKIKKDFC FSYVEEPNKQ
     EFLDFKQKYL DFSRNKAPKA NLSNALEEQL KENFKKLYND LFDGAIIRCD FFVIENEVYL
     NEINPIPGSL ANYLFDDFKT TLENLAQSLP KTPKIQIKNS YLLQIQKNK
//
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