ID Q9EU36_ENTFC Unreviewed; 342 AA. AC Q9EU36; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 03-APR-2013, entry version 73. DE RecName: Full=D-alanine--D-alanine ligase; DE EC=6.3.2.4; DE AltName: Full=D-Ala-D-Ala ligase; DE AltName: Full=D-alanylalanine synthetase; GN Name=vanB2; Synonyms=ddl; OS Enterococcus faecium (Streptococcus faecium). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1352; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CG4248; RA Lu J.-J., Perng C.-L., Ho M.-F.; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CG4248; RX PubMed=11376048; DOI=10.1128/JCM.39.6.2140-2145.2001; RA Lu J.J., Perng C.L., Ho M.F., Chiueh T.S., Lee W.H.; RT "High prevalence of VanB2 vancomycin-resistant Enterococcus faecium in RT Taiwan."; RL J. Clin. Microbiol. 39:2140-2145(2001). 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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF310957; AAG34693.1; -; Genomic_DNA. DR HSSP; P25051; 1E4E. DR ProteinModelPortal; Q9EU36; -. DR SMR; Q9EU36; 2-341. DR UniPathway; UPA00219; -. DR GO; GO:0005618; C:cell wall; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 2. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_00047; Dala_Dala_lig; 1; -. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. 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; IPR016185; PreATP-grasp_dom. DR PANTHER; PTHR23132; PTHR23132; 1. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 1. DR SUPFAM; SSF52440; PreATP-grasp-like; 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; Cytoplasm; KW Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Peptidoglycan synthesis. FT DOMAIN 136 337 ATP-grasp (By similarity). FT NP_BIND 162 215 ATP (By similarity). FT METAL 291 291 Magnesium or manganese 1 (By similarity). FT METAL 304 304 Magnesium or manganese 1 (By similarity). FT METAL 304 304 Magnesium or manganese 2 (By similarity). FT METAL 306 306 Magnesium or manganese 2 (By similarity). SQ SEQUENCE 342 AA; 37072 MW; 455EE3AE89C3A31A CRC64; MNRIKVATIF GGCSEEHDVS VKSAIEIAAN IDTEKFDPHY IGITKNGVWK LCKKPCTEWE ADSLPAILSP DRKTHGLLVM KESEYETRRI DVAFPVLHGK CGEDGAIQGL FVLSGIPYVG CDIQSSAACM DKSLAYILTK NAGIAVPEFQ MIDKGDKPEA GALTYPVFVK PARSGSSFGV TKVNGPEELN AAIEAAGQYD GKILIEQAIS GCEVGCAVMG NEDDLIVGEV DQIRLSHGIF RIHQENEPEK GSENAMITVP ADIPVEERNR VQETAKKVYR VLGCRGLARV DLFLQEDGGI VLNEVNTMPG FTSYSRYPRM VAAAGITLPA LIDSLITLAL KR //