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Database: UniProt
Entry: Q8KCR8
LinkDB: Q8KCR8
Original site: Q8KCR8 
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
//
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