GenomeNet

Database: UniProt
Entry: Q3B391
LinkDB: Q3B391
Original site: Q3B391 
ID   DDL_PELLD               Reviewed;         361 AA.
AC   Q3B391;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   19-FEB-2014, entry version 62.
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=Plut_1331;
OS   Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM
OS   273)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=319225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 273;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelodictyon luteolum DSM 273.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000096; ABB24190.1; -; Genomic_DNA.
DR   RefSeq; YP_375233.1; NC_007512.1.
DR   ProteinModelPortal; Q3B391; -.
DR   STRING; 319225.Plut_1331; -.
DR   EnsemblBacteria; ABB24190; ABB24190; Plut_1331.
DR   GeneID; 3744483; -.
DR   KEGG; plt:Plut_1331; -.
DR   PATRIC; 21380284; VBIChlLut1287_1401.
DR   eggNOG; COG1181; -.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; MDKIAMK; -.
DR   OrthoDB; EOG64BQ73; -.
DR   ProtClustDB; PRK01966; -.
DR   BioCyc; PLUT319225:GHDM-1340-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-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; 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.
FT   CHAIN         1    361       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_1000030477.
FT   DOMAIN      144    350       ATP-grasp.
FT   NP_BIND     177    232       ATP (By similarity).
FT   METAL       303    303       Magnesium or manganese 1 (By similarity).
FT   METAL       317    317       Magnesium or manganese 1 (By similarity).
FT   METAL       317    317       Magnesium or manganese 2 (By similarity).
FT   METAL       319    319       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   361 AA;  38707 MW;  B3EB96E244C0ED90 CRC64;
     MHHTTVALLF GGRSLEHEIS VISARAVAAN IDRDRYRVLA VYITRDGGWY AGGVAEQILK
     LDIADLIRTT SLEATAATLR EMVAASAEPP FNFDFRGIDV AFPVLHGSYG EDGRVQGLLE
     TLQVPCTGCG VLASALTMDK ALTKLAAADA GLAVAVSVTV MSHAYRRDPE ATHRLAVASL
     SFPMFVKPVS LGSSVGITKV NSESELAEAI THACSLDSKV LIEQAVKGRE VEVAVIGNDT
     LEASPCGEIE PGSEFYDYED KYIHDTAKLF IPARIPGDLQ EKVREAALCA YRALGCRGMS
     RVDFFVDETT GSIVFNEINT IPGFTPVSMY PRLMAAAGTG FMELTDRLIR LAMEPEAGAS
     A
//
DBGET integrated database retrieval system