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Database: UniProt/SWISS-PROT
Entry: DDLB_PSESM
LinkDB: DDLB_PSESM
Original site: DDLB_PSESM 
ID   DDLB_PSESM              Reviewed;         319 AA.
AC   Q87WY7;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   28-FEB-2018, entry version 106.
DE   RecName: Full=D-alanine--D-alanine ligase B {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 B {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase B {ECO:0000255|HAMAP-Rule:MF_00047};
GN   Name=ddlB {ECO:0000255|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=PSPTO_4406;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F.,
RA   Madupu R., Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H.,
RA   Nelson W.C., Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q.,
RA   Khouri H.M., Fedorova N.B., Tran B., Russell D., Berry K.J.,
RA   Utterback T.R., Van Aken S.E., Feldblyum T.V., D'Ascenzo M.,
RA   Deng W.-L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K.,
RA   Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X.,
RA   Bender C.L., White O., Fraser C.M., Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {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; AE016853; AAO57855.1; -; Genomic_DNA.
DR   RefSeq; NP_794160.1; NC_004578.1.
DR   RefSeq; WP_011105003.1; NC_004578.1.
DR   ProteinModelPortal; Q87WY7; -.
DR   SMR; Q87WY7; -.
DR   STRING; 223283.PSPTO_4406; -.
DR   EnsemblBacteria; AAO57855; AAO57855; PSPTO_4406.
DR   GeneID; 1186087; -.
DR   KEGG; pst:PSPTO_4406; -.
DR   PATRIC; fig|223283.9.peg.4521; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; MQGLLEC; -.
DR   OrthoDB; POG091H00GT; -.
DR   PhylomeDB; Q87WY7; -.
DR   BioCyc; PSYR223283:G1G0D-4472-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002515; 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-EC.
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-UniPathway.
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    319       D-alanine--D-alanine ligase B.
FT                                /FTId=PRO_0000177860.
FT   DOMAIN      117    312       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     143    198       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       266    266       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       279    279       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       279    279       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       281    281       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   319 AA;  34087 MW;  AD31868A3E161061 CRC64;
     MTAVARSSLR STLEPKSFGR VAVLFGGKSA EREVSLNSGN AVLKALLDAG VDAFGIDVGD
     DFLQRLVSEK IDRAFIVLHG RGGEDGTMQG LLECLEIPYT GSGVLASALA MDKLRTKQVW
     QSLGPATPLH AVLENENDCI CAATELGFPL IVKPAHEGSS IGMAKVNSVD ELIAAWKAAS
     TYDSQVLVEQ WIQGPEFTVA SLRGQVLPPI GLGTPHSFYD YDAKYLASDT QYRIPCGLDD
     AQEQQLKQLA ARACDAIGIA GWARTDVMQD AEGKFWLLEV NTVPGMTDHS LVPMAARAAG
     LNFQQLVLAI LADSVQARG
//
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