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Database: UniProt
Entry: B2GFL1
LinkDB: B2GFL1
Original site: B2GFL1 
ID   DDL_KOCRD               Reviewed;         383 AA.
AC   B2GFL1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   16-JAN-2019, entry version 68.
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};
GN   OrderedLocusNames=KRH_10370;
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 /
OS   DC2201).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N.,
RA   Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria
RT   rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
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; AP009152; BAG29384.1; -; Genomic_DNA.
DR   RefSeq; WP_012398105.1; NC_010617.1.
DR   ProteinModelPortal; B2GFL1; -.
DR   SMR; B2GFL1; -.
DR   STRING; 378753.KRH_10370; -.
DR   EnsemblBacteria; BAG29384; BAG29384; KRH_10370.
DR   GeneID; 35827368; -.
DR   KEGG; krh:KRH_10370; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   OrthoDB; 764798at2; -.
DR   BioCyc; KRHI378753:G1G2M-1033-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008838; 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    383       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_1000091188.
FT   DOMAIN      164    373       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     196    251       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       327    327       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       340    340       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       340    340       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       342    342       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   383 AA;  41365 MW;  06B548C65AB11521 CRC64;
     MSTTHETPEA TAEGDKPCIA VVFGGRSSEH SISLITARSV LRAIDRDRWD VVSVGISTDG
     AWFLCSQEEL EALLDDQPMA QLPVGVHRVS LPLQTGDSRL LIHDTSEHGA PLSRGRHIDA
     VFPLLHGPFG EDGTLQGMLE LADLPYVGCG VAASAIGMDK HFMKLAFQAA GLEVGPYTVV
     HDRTWRTDPL GVREAVAELG FPVFVKPARA GSSFGITRVD EPSQLDAAIA TAREHDLKLV
     VEAGIDGREI ECAVLGGHGT DEARASLPGE IEVHGHALYD FEAKYVESDG ATLSCPARLP
     EHVIDTLRRD AVRAFHAVDG EGLSRCDFFV TADERVLINE INTMPGFTPI SMYPRMWAAS
     GIDYSALIDE LITLALERPV GLR
//
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