ID Q9EU36_ENTFC Unreviewed; 342 AA. AC Q9EU36; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 14-APR-2009, entry version 49. DE SubName: Full=Ligase VanB2; GN Name=vanB2; OS Enterococcus faecium (Streptococcus faecium). OC Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus. OX NCBI_TaxID=1352; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CG4248; RX MEDLINE=21270249; PubMed=11376048; RX 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). RN [2] 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. 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: 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 SMR; Q9EU36; 2-341. DR GO; GO:0005618; C:cell wall; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro. 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:InterPro. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 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; Cytoplasm; KW Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Peptidoglycan synthesis. 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 //