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Database: UniProt/TrEMBL
Entry: E6NDL2_HELPI
LinkDB: E6NDL2_HELPI
Original site: E6NDL2_HELPI 
ID   E6NDL2_HELPI            Unreviewed;       347 AA.
AC   E6NDL2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   25-OCT-2017, entry version 49.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
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   ECO:0000313|EMBL:BAJ55222.1};
GN   OrderedLocusNames=HPF16_0625 {ECO:0000313|EMBL:BAJ55222.1};
OS   Helicobacter pylori (strain F16).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=866344 {ECO:0000313|EMBL:BAJ55222.1, ECO:0000313|Proteomes:UP000007935};
RN   [1] {ECO:0000313|EMBL:BAJ55222.1, ECO:0000313|Proteomes:UP000007935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F16 {ECO:0000313|EMBL:BAJ55222.1,
RC   ECO:0000313|Proteomes:UP000007935};
RX   PubMed=21575176; DOI=10.1186/1471-2180-11-104;
RA   Kawai M., Furuta Y., Yahara K., Tsuru T., Oshima K., Handa N.,
RA   Takahashi N., Yoshida M., Azuma T., Hattori M., Uchiyama I.,
RA   Kobayashi I.;
RT   "Evolution in an oncogenic bacterial species with extreme genome
RT   plasticity: Helicobacter pylori East Asian genomes.";
RL   BMC Microbiol. 11:104-104(2011).
RN   [2] {ECO:0000313|EMBL:BAJ55222.1, ECO:0000313|Proteomes:UP000007935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F16 {ECO:0000313|EMBL:BAJ55222.1,
RC   ECO:0000313|Proteomes:UP000007935};
RX   PubMed=21212362; DOI=10.1073/pnas.1012579108;
RA   Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T.,
RA   Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I.,
RA   Kobayashi I.;
RT   "Birth and death of genes linked to chromosomal inversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910576}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910566}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00910571};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00910564};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910582}.
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:SAAS00910642}.
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DR   EMBL; AP011940; BAJ55222.1; -; Genomic_DNA.
DR   RefSeq; WP_000393694.1; NC_017368.1.
DR   EnsemblBacteria; BAJ55222; BAJ55222; HPF16_0625.
DR   KEGG; hef:HPF16_0625; -.
DR   PATRIC; fig|866344.4.peg.662; -.
DR   KO; K01921; -.
DR   OMA; YDTKYIN; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000007935; 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:UP000007935};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00910562};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741};
KW   Magnesium {ECO:0000256|SAAS:SAAS00910568};
KW   Manganese {ECO:0000256|SAAS:SAAS00910578};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00910590};
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      134    332       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   347 AA;  39537 MW;  CFB948590AE4486E CRC64;
     MEFCVLFGGA SFEYEISIVS AIALKEALKD RIKYFIFLDE NHHFYLIEES NMHSKYFAQI
     KEKKLPPLIL THNGLLKSSF LGAKTIELPL VINLVHGGDG EDGKLASLLE FYRIAFIGPR
     IEASVLSYNK YLTKLYAKDL GVKALDYVLL NEKNCANALN LIGFNFPFII KPSNAGSSLG
     VSVVKEEKEL IYALDGAFEY SKEVLIEPFI QGVKEYNLAG CKIKKDFCFS YVEEPNKQEF
     LDFKQKYLDF SRNKAPKANL SSALEEQLKE NFKKLYNDLF DGALIRCDFF VIENEVYLNE
     INPIPGSLAN YLFDDFKTTL ENLAQSLPKT PKIPIKNSYL LQIQKNK
//
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