ID DDLB_SALTI Reviewed; 306 AA. AC Q8Z9G7; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 25-NOV-2008, entry version 56. DE RecName: Full=D-alanine--D-alanine ligase B; DE EC=6.3.2.4; DE AltName: Full=D-alanylalanine synthetase B; DE AltName: Full=D-Ala-D-Ala ligase B; GN Name=ddlB; OrderedLocusNames=STY0150, t0134; OS Salmonella typhi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18; RX MEDLINE=21534947; PubMed=11677608; DOI=10.1038/35101607; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., RA Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J., RA Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., RA Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., RA Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., RA Whitehead S., Barrell B.G.; RT "Complete genome sequence of a multiple drug resistant Salmonella RT enterica serovar Typhi CT18."; RL Nature 413:848-852(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700931 / Ty2; RX MEDLINE=22531367; PubMed=12644504; RX DOI=10.1128/JB.185.7.2330-2337.2003; RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., RA Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.; RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 RT and CT18."; RL J. Bacteriol. 185:2330-2337(2003). 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 -!- SUBUNIT: Monomer (By similarity). 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; AL627265; CAD01287.1; -; Genomic_DNA. DR EMBL; AE014613; AAO67866.1; -; Genomic_DNA. DR RefSeq; NP_454742.1; -. DR RefSeq; NP_804017.1; -. DR HSSP; P07862; 1IOW. DR SMR; Q8Z9G7; 1-306. DR GeneID; 1067715; -. DR GeneID; 1246645; -. DR GenomeReviews; AL513382_GR; STY0150. DR GenomeReviews; AE014613_GR; t0134. DR KEGG; stt:t0134; -. DR KEGG; sty:STY0150; -. DR HOGENOM; Q8Z9G7; -. DR BioCyc; SENT209261:T0134-MON; -. DR BioCyc; SENT220341:STY0150-MON; -. DR GO; GO:0005618; C:cell wall; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00047; -; 1. DR InterPro; IPR011761; ATP-grasp. 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; IPR013817; Pre-ATP_grasp. DR Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1. DR Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 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 INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 306 D-alanine--D-alanine ligase B. FT /FTId=PRO_0000177869. FT DOMAIN 101 303 ATP-grasp. FT NP_BIND 134 189 ATP (By similarity). FT METAL 257 257 Magnesium or manganese 1 (By similarity). FT METAL 270 270 Magnesium or manganese 1 (By similarity). FT METAL 270 270 Magnesium or manganese 2 (By similarity). FT METAL 272 272 Magnesium or manganese 2 (By similarity). SQ SEQUENCE 306 AA; 32650 MW; 241275EB0D9D10B5 CRC64; MADKIAVLLG GTSAERDVSL NSGAAVLAGL REGGIDAHPV DPQEVDVAQL KAMGFQKVFI ALHGRGGEDG TLQGMLELLG LPYTGSGVMA SALSMDKLRS KLLWQGAGLP VAPWVALTRA EFEKGLSEEQ KARISALGLP LIVKPSREGS SVGMTKVVEE NALQGALSLA FQHDDEILIE KWLCGPEFTV AIVGEEILPS IRIQPAGTFY DYEAKYLSDE TQYFCPAGLE ASQEAALQSL VLQAWKALGC TGWGRIDVML DSDGQFYLLE ANTSPGMTSH SLVPMAARQA GMSFSQLVVR ILELAD //