ID DDL_PSEPG Reviewed; 318 AA.
AC B0KFS4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 29-MAY-2013, entry version 39.
DE RecName: Full=D-alanine--D-alanine ligase;
DE EC=6.3.2.4;
DE AltName: Full=D-Ala-D-Ala ligase;
DE AltName: Full=D-alanylalanine synthetase;
GN Name=ddl; OrderedLocusNames=PputGB1_4510;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC alanyl-D-alanine.
CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR EMBL; CP000926; ABZ00397.1; -; Genomic_DNA.
DR RefSeq; YP_001670732.1; NC_010322.1.
DR ProteinModelPortal; B0KFS4; -.
DR STRING; 76869.PputGB1_4510; -.
DR EnsemblBacteria; ABZ00397; ABZ00397; PputGB1_4510.
DR GeneID; 5872317; -.
DR KEGG; ppg:PputGB1_4510; -.
DR PATRIC; 19936099; VBIPsePut76638_4514.
DR eggNOG; COG1181; -.
DR HOGENOM; HOG000011592; -.
DR KO; K01921; -.
DR OMA; WREAARY; -.
DR ProtClustDB; PRK01372; -.
DR BioCyc; PPUT76869:GIXB-4587-MONOMER; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 2.
DR Gene3D; 3.40.50.20; -; 1.
DR HAMAP; MF_00047; Dala_Dala_lig; 1; -.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
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 PANTHER; PTHR23132; PTHR23132; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01820; Dala_Dala_lig_N; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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 1 318 D-alanine--D-alanine ligase.
FT /FTId=PRO_1000074780.
FT DOMAIN 116 311 ATP-grasp.
FT NP_BIND 142 197 ATP (By similarity).
FT METAL 265 265 Magnesium or manganese 1 (By similarity).
FT METAL 278 278 Magnesium or manganese 1 (By similarity).
FT METAL 278 278 Magnesium or manganese 2 (By similarity).
FT METAL 280 280 Magnesium or manganese 2 (By similarity).
SQ SEQUENCE 318 AA; 34060 MW; D608F68A35ECB267 CRC64;
MTSAYDKLHS TLDVKAFGRV AVLYGGKSAE REVSLKSGAA VIDALTTAGV DVVAIDVGDD
LLARLQSEEI DRAFIILHGR GGEDGSMQGL LECLGIPYTG SGILASALAM DKLRTKQVWQ
SLGIPTPRHA VLASESDCLQ ASTELGFPLI VKPAHEGSSI GMAKVNSAQE LVAAWQDAAK
YDSQVLVEQW IHGPEFTIAV LRGQVLPPIA LGTPHVFYDY DAKYIANDTQ YRIPCGLDSA
KEQELIDLTA RACDAIGIEG WGRLDVMQDE QGRFWLLEVN TAPGMTDHSL VPMAARAAGL
DFQQLVLAIL AESVATRG
//
