ID A0A0H0VV97_BRAHO Unreviewed; 462 AA. AC A0A0H0VV97; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 14-OCT-2015, entry version 2. DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00046}; DE EC=6.3.2.8 {ECO:0000256|HAMAP-Rule:MF_00046}; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000256|HAMAP-Rule:MF_00046}; GN Name=murC {ECO:0000256|HAMAP-Rule:MF_00046}; GN ORFNames=SZ40_12035 {ECO:0000313|EMBL:KLI41654.1}; OS Brachyspira hyodysenteriae (Treponema hyodysenteriae). OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=159 {ECO:0000313|EMBL:KLI41654.1, ECO:0000313|Proteomes:UP000035148}; RN [1] {ECO:0000313|EMBL:KLI41654.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Q17 {ECO:0000313|EMBL:KLI41654.1}; RA Black M.L., Moolhuijzen P.M., Barrero R., La T., Phillips N.D., RA Hampson D.J., Herbst W., Barth S., Bellgard M.I.; RT "Analysis of multiple Brachyspira hyodysenteriae genomes confirms that RT the species is relatively conserved but has potentially important RT strain variation."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramate + L- CC alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- CC alanine. {ECO:0000256|HAMAP-Rule:MF_00046}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00046}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00046}. CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP- CC Rule:MF_00046}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLI41654.1}. 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; JXNM01000106; KLI41654.1; -; Genomic_DNA. DR RefSeq; WP_012669863.1; NZ_JXNM01000106.1. DR GeneID; 24365497; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000035148; Unassembled WGS sequence. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00046}; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00046}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00046}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00046}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00046}; KW Complete proteome {ECO:0000313|Proteomes:UP000035148}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00046}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000313|EMBL:KLI41654.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00046}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00046}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT NP_BIND 114 120 ATP. {ECO:0000256|HAMAP-Rule:MF_00046}. SQ SEQUENCE 462 AA; 51135 MW; C8C25B038BEA8CC3 CRC64; MFTKRKEKIH FIGIGGIGMS AIASVLNAIG FTITGSDLAK TAKTESLESS GIKVYYGHKA QNIEDDVTAV VTSSAISPTN EEIIEAKSKK ITVISRGEML AELMRLRYGI AISGSHGKTT TTSLISQIMM HAGLNPVCII GGNHFNLKSN AACNDLSSEY MVCEADESDG SFLRLSPVIN VVTNIDNDHL DYYGNVEALR VAFLEFINKV PFYGCSFLCF EDNVVKDLSK SANKKYYSYG FSKDYDFYVD RDSIRVEAPI TYFTAYHNSE CLGEFSVPLI GIHNVLNSLA SIGVGIHLGI DIADIKEGLK TFEGVGRRLN KLYDKEITLF DDYAHHPTEI KATLSSVRNA YKNRRIIAVF QPHRYSRTEL LLNDFEYAFN DADEVIISDI YAAGESPIPG ISGEIICDVV RKQNNHVRYI PNIEDVLPVL DDIKKDGDII LTLGAGNIVR ISNEYARKLQ NG //