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Database: UniProt/TrEMBL
Entry: E1PZJ7_HELPM
LinkDB: E1PZJ7_HELPM
Original site: E1PZJ7_HELPM 
ID   E1PZJ7_HELPM            Unreviewed;       347 AA.
AC   E1PZJ7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   25-OCT-2017, entry version 51.
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:ADO02338.1};
GN   OrderedLocusNames=HPSJM_03740 {ECO:0000313|EMBL:ADO02338.1};
OS   Helicobacter pylori (strain SJM180).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=765962 {ECO:0000313|EMBL:ADO02338.1, ECO:0000313|Proteomes:UP000006862};
RN   [1] {ECO:0000313|Proteomes:UP000006862}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJM180 {ECO:0000313|Proteomes:UP000006862};
RA   Kersulyte D., Velapatino B., Gilman R.H., Berg D.E.;
RT   "Complete genome sequence of Helicobacter pylori strain SJM180.";
RL   Submitted (JUN-2010) 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; CP002073; ADO02338.1; -; Genomic_DNA.
DR   RefSeq; WP_000393685.1; NC_014560.1.
DR   EnsemblBacteria; ADO02338; ADO02338; HPSJM_03740.
DR   KEGG; hpm:HPSJM_03740; -.
DR   HOGENOM; HOG000102494; -.
DR   KO; K01921; -.
DR   OMA; YDTKYIN; -.
DR   OrthoDB; POG091H06GK; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000006862; 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:UP000006862};
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, ECO:0000313|EMBL:ADO02338.1};
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;  39752 MW;  3132806CE663B6D3 CRC64;
     MEFCVLFGGA SFEHEISIVS AIVLKGVLKD RIKYFIFLDE NHHFYLIEES NMHSKYFAQI
     KEKKLPPLML THNGLLKNSF LGAKIIELPL VINLVHGGDG EDGKLASLLE FYRIAFIGPR
     IEASVLSYNK YLTKLYAKDL GVKTLDYILL NEKNRANALD LIGFNFPFIV KPSNAGSSLG
     VNVVKEEKEL NYALDSAFEY SKEVLIEPFI QGVKEYNLAG CKIKKDFCFS YIEEPNKQEF
     LDFKQKYLDF SRTKAPKANL SNALEKQLKE NFKKLYNDLF DGAIIRCDFF VIENEVYLNE
     INPIPGSLAN YLFDDFKTTL ENLAQSLPKT PKIQIKNSYL LQIQKNK
//
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