ID DDL_CHLTE Reviewed; 364 AA.
AC Q8KCR8;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 16-JAN-2019, entry version 103.
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}; Synonyms=ddlA;
GN OrderedLocusNames=CT1345;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 /
OS TLS) (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a
RT photosynthetic, anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM72574.1; -; Genomic_DNA.
DR RefSeq; NP_662232.1; NC_002932.3.
DR RefSeq; WP_010933013.1; NC_002932.3.
DR ProteinModelPortal; Q8KCR8; -.
DR SMR; Q8KCR8; -.
DR STRING; 194439.CT1345; -.
DR PRIDE; Q8KCR8; -.
DR EnsemblBacteria; AAM72574; AAM72574; CT1345.
DR GeneID; 1006715; -.
DR KEGG; cte:CT1345; -.
DR PATRIC; fig|194439.7.peg.1224; -.
DR eggNOG; ENOG4105CPF; Bacteria.
DR eggNOG; COG1181; LUCA.
DR HOGENOM; HOG000011593; -.
DR KO; K01921; -.
DR OMA; YETKYTE; -.
DR OrthoDB; 764798at2; -.
DR BioCyc; CTEP194439:G1FZE-1383-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001007; 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;
KW Reference proteome.
FT CHAIN 1 364 D-alanine--D-alanine ligase.
FT /FTId=PRO_0000177803.
FT DOMAIN 146 352 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00047}.
FT NP_BIND 179 234 ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 305 305 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 319 319 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 319 319 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 321 321 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ SEQUENCE 364 AA; 39033 MW; C8565880E5A01F7B CRC64;
MSKQTVALFF GGKSAEHEIS IISARSIAAQ IDRNRYELSP LYIDRDGKWH ASECSQQVLD
TDIAALLRSG TPESAGKRLD ELTAAAAGEC FDFGSFLKNT DVAFIALHGS YGEDGKLQGC
LDTFGIPYTG CGLTASALAM DKVLTKLCAM NAGIAVAEFM TITSCAYMAN PLETIVEITK
RFDWPLFVKP ASLGSSVGIS KVRNAEELAA ALENACGLDS KALVEAAISG REIEVAVLGN
SDPLASEPGE IIPGSDFYSY EDKYIKNEAK IVIPADLPEG VAEEVRKAAL TVFKALGCEG
MARVDFFVEN GTNRVILNEI NTIPGFTDIS MYPMMMAASG IGFAELVEKL LLLALEKRSI
THKI
//
