GenomeNet

Database: UniProt/TrEMBL
Entry: X2IF02_HELPX
LinkDB: X2IF02_HELPX
Original site: X2IF02_HELPX 
ID   X2IF02_HELPX            Unreviewed;       356 AA.
AC   X2IF02;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-SEP-2017, entry version 25.
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=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   ORFNames=HPOKI673_03725 {ECO:0000313|EMBL:AHN41953.1};
OS   Helicobacter pylori oki673.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1382925 {ECO:0000313|EMBL:AHN41953.1, ECO:0000313|Proteomes:UP000019661};
RN   [1] {ECO:0000313|EMBL:AHN41953.1, ECO:0000313|Proteomes:UP000019661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oki673 {ECO:0000313|EMBL:AHN41953.1};
RX   PubMed=24744331;
RA   Satou K., Shiroma A., Teruya K., Shimoji M., Nakano K., Juan A.,
RA   Tamotsu H., Terabayashi Y., Aoyama M., Teruya M., Suzuki R.,
RA   Matsuda M., Sekine A., Kinjo N., Kinjo F., Yamaoka Y., Hirano T.;
RT   "Complete Genome Sequences of Eight Helicobacter pylori Strains with
RT   Different Virulence Factor Genotypes and Methylation Profiles,
RT   Isolated from Patients with Diverse Gastrointestinal Diseases on
RT   Okinawa Island, Japan, Determined Using PacBio Single-Molecule Real-
RT   Time Technology.";
RL   Genome Announc. 2:e00286-14(2014).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP006825; AHN41953.1; -; Genomic_DNA.
DR   EnsemblBacteria; AHN41953; AHN41953; HPOKI673_03725.
DR   KEGG; hpyg:HPOKI673_03725; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000019661; 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:UP000019661};
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:AHN41953.1};
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      143    341       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   356 AA;  40653 MW;  3D1E3DD7C704A088 CRC64;
     MQSFLGSLIV EFCVLFGGAS FEHEISIVSA IALKEALKDR IKYFIFLDEN HHFYLIEESN
     MHSKYFAQIK EKKLPPLILT RNGLLKNSFL GAKIIELPLV INLVHGGDGE DGKLASLLEF
     YRIAFIGPRI EASVLSYNKY LTKLYAKDLG VKTLDYVLLN EKNRTNALNL IGFNFPFIVK
     PSNAGSSLGV SVVKEEKELI YALDGAFEYS KEVLIEPFIQ GVKEYNLAGC KIKKDFCFSY
     IEEPNKQEFL DFKQKYLDFS RNKAPKANLS NALEEQLKEN FKKLYNDLFD GALIRCDFFV
     IENKVYLNEI NPIPGSLANY LFDDFKTTLE NLAQSLPKTP KIPIKNSYLL QIQKNK
//
DBGET integrated database retrieval system