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Database: UniProt
Entry: A0M4U5
LinkDB: A0M4U5
Original site: A0M4U5 
ID   DDL_GRAFK               Reviewed;         326 AA.
AC   A0M4U5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JAN-2019, entry version 83.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE            EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=GFO_2684;
OS   Gramella forsetii (strain KT0803).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gramella.
OX   NCBI_TaxID=411154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT0803;
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
CC         phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00047};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00047}.
DR   EMBL; CU207366; CAL67640.1; -; Genomic_DNA.
DR   RefSeq; WP_011710543.1; NC_008571.1.
DR   ProteinModelPortal; A0M4U5; -.
DR   SMR; A0M4U5; -.
DR   STRING; 411154.GFO_2684; -.
DR   EnsemblBacteria; CAL67640; CAL67640; GFO_2684.
DR   KEGG; gfo:GFO_2684; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   OrthoDB; 764798at2; -.
DR   BioCyc; GFOR411154:G1GJG-2549-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000755; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   PIRSF; PIRSF039102; Ddl/VanB; 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; Cell shape; Cell wall biogenesis/degradation;
KW   Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    326       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341104.
FT   DOMAIN      121    320       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     149    204       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       275    275       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       287    287       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       287    287       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       289    289       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   326 AA;  36436 MW;  15D631E2BC685E20 CRC64;
     MKKKIAIAMG GYSSEYRISI NSGNIVYKHL DHDLYEPYRV HILKGEWFVV ADDDTPYPIN
     KSNFTVKIND KVIQFDCVFN TIHGTPGENG LLQAYLELIG IPQTSCDYYQ SALTFNKRDL
     ISVLRPYGIK AATNYFLNKD QEINTKEIVD KVGLPCFVKA NRAGSSFGVT KVKTEDEIIS
     AAKTAFTEDD EAIIESFLDG TEVSVGVITY KGKVLALPVT EIIPDGEFFD YEAKYLGKSQ
     EITPARISEE DTKKVQDIAI MIYKKLKMKG LSRSEFIFHE GEPHFIEMNT NPGISQASIL
     PQQAEKAGIS LKDLFGSTIE AALNQK
//
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