ID DDL_BACHD Reviewed; 305 AA.
AC Q9KCF0;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 29-MAY-2013, entry version 86.
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; Synonyms=ddlA; OrderedLocusNames=BH1621;
OS Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM
OS 9153 / C-125).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT halodurans and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- FUNCTION: Cell wall formation (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC alanyl-D-alanine.
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; BA000004; BAB05340.1; -; Genomic_DNA.
DR PIR; E83852; E83852.
DR RefSeq; NP_242487.1; NC_002570.2.
DR ProteinModelPortal; Q9KCF0; -.
DR STRING; 272558.BH1621; -.
DR EnsemblBacteria; BAB05340; BAB05340; BAB05340.
DR GeneID; 891998; -.
DR KEGG; bha:BH1621; -.
DR PATRIC; 18940356; VBIBacHal18977_1691.
DR eggNOG; COG1181; -.
DR HOGENOM; HOG000011592; -.
DR KO; K01921; -.
DR OMA; ITRHESE; -.
DR ProtClustDB; CLSK2300057; -.
DR BioCyc; BHAL272558:GJC5-1705-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:0046872; F:metal ion binding; IEA:InterPro.
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; atypical.
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; Nucleotide-binding;
KW Peptidoglycan synthesis.
FT CHAIN 1 305 D-alanine--D-alanine ligase.
FT /FTId=PRO_0000177784.
FT DOMAIN 99 300 ATP-grasp.
FT NP_BIND 126 181 ATP (By similarity).
SQ SEQUENCE 305 AA; 33126 MW; C806D03993D3D081 CRC64;
MKIAVLYGGT SAEREVSLSS GKGIMEALKA NGHEVIGIDF HPDQVRDLVD LDVDLVFIGL
HGRLGEDGKV QALLDLLNIP YVGTGVQGSA LAMDKAKAKL FFEKAGIRVA EEVVLHSFTY
DANAFNFTGT YPVVVKPNQE GSTIGLTVAE TEEELLQGIE EAFRHDDTIL IEEFIAGTEV
TVAVLGNKGE ERSLPVVEIV PKNKLYDYES KYAPGMSEHI VPARISEEHT AYVQQAAVRA
HQALGCDVYS RVDFIVPNDG SDPVILKVNT LPGMTPTSLY PDAAKGVGMS YEEMIQTFVN
LSLKK
//
