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Database: UniProt/TrEMBL
Entry: D0JZD7_HELP5
LinkDB: D0JZD7_HELP5
Original site: D0JZD7_HELP5 
ID   D0JZD7_HELP5            Unreviewed;       347 AA.
AC   D0JZD7;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   28-MAR-2018, entry version 57.
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:ACX99207.1};
GN   OrderedLocusNames=HPKB_0610 {ECO:0000313|EMBL:ACX99207.1};
OS   Helicobacter pylori (strain 52).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=684950 {ECO:0000313|EMBL:ACX99207.1, ECO:0000313|Proteomes:UP000002568};
RN   [1] {ECO:0000313|Proteomes:UP000002568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=52 {ECO:0000313|Proteomes:UP000002568};
RA   Kim S., Lee W.K., Choi S.H., Kang S., Park H.S., Kim Y.S., Lee S.G.,
RA   Byun E.Y., Jeong J.E., Park Y.H., Lee E.J., Kim J.S., Ryu B.D.,
RA   Lee Y.S., Hahn Y., Yeom Y.I., Park S.G., Youn H.S., Ko G.H.,
RA   Choi M.B., Park C.H., Lim J.Y., Bae D.W., Song J.Y., Park J.U.,
RA   Kang H.L., Baik S.C., Cho M.J., Yoo H.S., Rhee K.H.;
RT   "Genome sequence of Helicobacter pylori strain 52.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001680; ACX99207.1; -; Genomic_DNA.
DR   RefSeq; WP_000393617.1; NC_017354.1.
DR   ProteinModelPortal; D0JZD7; -.
DR   EnsemblBacteria; ACX99207; ACX99207; HPKB_0610.
DR   KEGG; hpz:HPKB_0610; -.
DR   PATRIC; fig|684950.4.peg.650; -.
DR   HOGENOM; HOG000102494; -.
DR   KO; K01921; -.
DR   OMA; RCDFFVI; -.
DR   BioCyc; HPYL684950:G1GFG-635-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002568; 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_sf.
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:UP000002568};
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;  39723 MW;  01B484B0816A6A93 CRC64;
     MEFCVLFGGA SFEHEISIVS AIALKEALKD RIKYFIFLDE NHHFYLIEES NMHSKYFAQI
     KEKKLPPLIL TRNGLLKNSF LGAKIIELPL VINLVHGGDG EDGKLASLLE FYRIAFIGPR
     IEASVLSYNK YLTKLYAKDL GVKTLDYVLL NEKNRANALN LIGFNFPFIV KPSNAGSSLG
     VSVVKEEKEL IYALDSAFEY SKEILIEPFI QGVKEYNLAG CKIKKDFCFS YIEEPNKQEF
     LDFKQKYLDF SRNKAPKANL SNALEEQLKE NFKKLYNDLF DGALIRCDFF VIENEVYLNE
     INPIPGSLAN YLFDDFKTTL ENLAQSLPKT PKIPIKNSYL LQIQKNK
//
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