GenomeNet

Database: UniProt/SWISS-PROT
Entry: DDLB_PSEPK
LinkDB: DDLB_PSEPK
Original site: DDLB_PSEPK 
ID   DDLB_PSEPK              Reviewed;         318 AA.
AC   Q88N74;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   30-AUG-2017, entry version 96.
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=PP_1339;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 /
OS   KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M.,
RA   Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K.,
RA   Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D.,
RA   Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S.,
RA   Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B.,
RA   Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the
RT   metabolically versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN66962.1; -; Genomic_DNA.
DR   RefSeq; NP_743498.1; NC_002947.4.
DR   RefSeq; WP_010952456.1; NC_002947.4.
DR   ProteinModelPortal; Q88N74; -.
DR   SMR; Q88N74; -.
DR   STRING; 160488.PP_1339; -.
DR   EnsemblBacteria; AAN66962; AAN66962; PP_1339.
DR   GeneID; 1044021; -.
DR   KEGG; ppu:PP_1339; -.
DR   PATRIC; fig|160488.4.peg.1418; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; MQGLLEC; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000556; 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.
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    318       D-alanine--D-alanine ligase B.
FT                                /FTId=PRO_0000177858.
FT   DOMAIN      116    311       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     142    197       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       265    265       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       278    278       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       278    278       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       280    280       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   318 AA;  34131 MW;  D43D416D65ACFBDF CRC64;
     MTSAYDKLHS TLDVKAFGRV AVLYGGKSAE REVSLKSGAA VIDALSTAGV DVVAIDVGDD
     LLARLQSEKI DRAFIILHGR GGEDGSMQGL LECLGIPYTG SGILASALAM DKLRTKQVWQ
     SLGIPTPRHA VLASESDCLQ ASTELGFPLI VKPAHEGSSI GMAKVNSTQE LVAAWQDAAK
     YDSQVLVEQW IHGPEFTIAV LRGQVLPPIA LGTPHVFYDY DAKYIVNDTQ YRIPCGLDSV
     KEQELIDLTA RACDAIGIEG WGRLDVMQDE QGRFWLLEVN TAPGMTDHSL VPMAARAAGL
     DFQQLVLAIL AESVATRG
//
DBGET integrated database retrieval system