ID DDL_THEMA Reviewed; 303 AA.
AC P46805;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 16-JAN-2019, entry version 138.
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}; OrderedLocusNames=TM_0259;
OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-118.
RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
RX PubMed=8547314;
RA Bouthier de la Tour C., Kaltoum H., Portemer C., Confalonieri F.,
RA Huber R., Duguet M.;
RT "Cloning and sequencing of the gene coding for topoisomerase I from
RT the extremely thermophilic eubacterium, Thermotoga maritima.";
RL Biochim. Biophys. Acta 1264:279-283(1995).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA68950.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR EMBL; AE000512; AAD35347.1; -; Genomic_DNA.
DR EMBL; U27841; AAA68950.1; ALT_INIT; Genomic_DNA.
DR PIR; B72400; B72400.
DR RefSeq; NP_228072.1; NC_000853.1.
DR RefSeq; WP_010865083.1; NZ_CP011107.1.
DR ProteinModelPortal; P46805; -.
DR SMR; P46805; -.
DR STRING; 243274.TM0259; -.
DR EnsemblBacteria; AAD35347; AAD35347; TM_0259.
DR GeneID; 897169; -.
DR KEGG; tma:TM0259; -.
DR eggNOG; ENOG4105CPF; Bacteria.
DR eggNOG; COG1181; LUCA.
DR InParanoid; P46805; -.
DR KO; K01921; -.
DR OMA; YETKYTE; -.
DR OrthoDB; 764798at2; -.
DR BRENDA; 6.3.2.4; 6331.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008183; 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; IBA:GO_Central.
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; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1 303 D-alanine--D-alanine ligase.
FT /FTId=PRO_0000177896.
FT DOMAIN 99 293 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00047}.
FT NP_BIND 125 176 ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 248 248 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 260 260 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 260 260 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 262 262 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ SEQUENCE 303 AA; 34250 MW; A6057C711DA77725 CRC64;
MRVALLMGGV SREREISLRS GERVKKALEK LGYEHTVFDV REDFLKKVDQ LKSFDVVFNV
LHGTFGEDGT LQAILDFLGI RYTGSDAFSS MICFDKLVTY RFLKGTVEIP DFVEIKEFMK
TSPLGYPCVV KPRREGSSIG VFVCESDEEF QHALKEDLPR YGSVIVQKYI PGREMTVSIL
ETEKGFEILP VLELRPKRRF YDYVAKYTKG ETEFILPAPL NPSEERLVKE MALKAFVEAG
CRGFGRVDGI FSDGRFYFLE INTVPGLTET SDLPASAKAG GIEFEELVEI ILKSAFLKEG
VRV
//
