ID DDL_THEEB Reviewed; 343 AA.
AC Q8DLH0;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 01-MAY-2013, entry version 72.
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=tll0523;
OS Thermosynechococcus elongatus (strain BP-1).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
RA Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC08075.1; -; Genomic_DNA.
DR RefSeq; NP_681313.1; NC_004113.1.
DR ProteinModelPortal; Q8DLH0; -.
DR STRING; 197221.tll0523; -.
DR EnsemblBacteria; BAC08075; BAC08075; BAC08075.
DR GeneID; 1012194; -.
DR KEGG; tel:tll0523; -.
DR PATRIC; 23926296; VBITheElo119873_0551.
DR eggNOG; COG1181; -.
DR HOGENOM; HOG000011593; -.
DR KO; K01921; -.
DR OMA; LLHGPFG; -.
DR ProtClustDB; PRK01966; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0005618; C:cell wall; IEA:InterPro.
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;
KW Reference proteome.
FT CHAIN 1 343 D-alanine--D-alanine ligase.
FT /FTId=PRO_0000177893.
FT DOMAIN 127 336 ATP-grasp.
FT NP_BIND 163 218 ATP (By similarity).
FT METAL 289 289 Magnesium or manganese 1 (By similarity).
FT METAL 303 303 Magnesium or manganese 1 (By similarity).
FT METAL 303 303 Magnesium or manganese 2 (By similarity).
FT METAL 305 305 Magnesium or manganese 2 (By similarity).
SQ SEQUENCE 343 AA; 37489 MW; 2D946251FD093BD5 CRC64;
MGRLRVGLLF GGRSREHEVS VVSAAAIAQA FAAGDNGDRY EVIPIYIEKD GRWRHTERVG
IPEGTAPESS LWQFPAVVDT IDVWFPIVHG PNGEDGTIQG LLELMQRPYV GSGVAASAIG
MDKILMKTVF GAIGLPQVPY VALQRSDLWS DPCRYNHLCD RIETELGYPC FVKPANLGSS
VGISKAKNRQ QLTTALEVAA ELDRRIIVEA GVVARELECA VLGNDKPQAS VVGEITYSSE
FYDYETKYTD GRAQLHIPAE IPPAVSEQIR SLSLQAFQAL GAAGLARFDF FYVPSTGEVL
INEVNTLPGF TALSMYPQLW AASGLSFPEL VHRLVQLALE WHA
//
