ID DDL_BARQU Reviewed; 306 AA. AC Q6FZ74; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 04-NOV-2008, entry version 40. DE RecName: Full=D-alanine--D-alanine ligase; DE EC=6.3.2.4; DE AltName: Full=D-alanylalanine synthetase; DE AltName: Full=D-Ala-D-Ala ligase; GN Name=ddl; OrderedLocusNames=BQ08830; OS Bartonella quintana (Rochalimaea quintana). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=803; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Toulouse; RX PubMed=15210978; DOI=10.1073/pnas.0305659101; RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., RA La Scola B., Holmberg M., Andersson S.G.E.; RT "The louse-borne human pathogen Bartonella quintana is a genomic RT derivative of the zoonotic agent Bartonella henselae."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004). 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; BX897700; CAF26362.1; -; Genomic_DNA. DR RefSeq; YP_032495.1; -. DR GeneID; 2867175; -. DR GenomeReviews; BX897700_GR; BQ08830. DR KEGG; bqu:BQ08830; -. DR NMPDR; fig|283165.1.peg.765; -. DR HOGENOM; Q6FZ74; -. DR BioCyc; BQUI283165:BQ08830-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. 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 CHAIN 1 306 D-alanine--D-alanine ligase. FT /FTId=PRO_1000030430. FT DOMAIN 102 300 ATP-grasp. FT NP_BIND 128 183 ATP (By similarity). FT METAL 253 253 Magnesium or manganese 1 (By similarity). FT METAL 267 267 Magnesium or manganese 1 (By similarity). FT METAL 267 267 Magnesium or manganese 2 (By similarity). FT METAL 269 269 Magnesium or manganese 2 (By similarity). SQ SEQUENCE 306 AA; 33288 MW; 1ACFFD24DB7374BD CRC64; MKGEHVAVLM GGGSSERSVS LSSGTACADI LEARGYRVSR VDVDSHIASV LERLQPDVAF NALHGPFGED GCIQGVLEYL KIPYTHSGVM ASALAMDKGR AKIVVASVGV SVAPSCIMSR FAVGREHPME PPYVIKPLCE GSSFGVVIVK ENESAPPRNV VGAEWVYADE VIVEKYIPGR EFTCAVLGNE ALDVCEIFPD KHFQFYNYDS KYKSGGSLHI CPAQLSPNIY QNVQRMSLAA HQAIGCRGVS RSDFRFNEET GELVWLEINT QPGMTPTSLF PDIAKASGRT YGDIVQWMVE DASCMR //