ID A0A0G0USN4_9BACT Unreviewed; 771 AA. AC A0A0G0USN4; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 17-FEB-2016, entry version 7. DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|SAAS:SAAS00243344}; DE EC=6.3.2.8 {ECO:0000256|SAAS:SAAS00243344}; GN ORFNames=UU43_C0002G0042 {ECO:0000313|EMBL:KKR91733.1}; OS Parcubacteria (Falkowbacteria) bacterium GW2011_GWA2_41_14. OC Bacteria; Parcubacteria; Falkowbacteria. OX NCBI_TaxID=1618635 {ECO:0000313|EMBL:KKR91733.1, ECO:0000313|Proteomes:UP000034190}; RN [1] {ECO:0000313|EMBL:KKR91733.1, ECO:0000313|Proteomes:UP000034190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: Cell wall formation. {ECO:0000256|SAAS:SAAS00243396}. 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|SAAS:SAAS00189116}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|SAAS:SAAS00085119}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00085149}. CC -!- SIMILARITY: Belongs to the MurCDEF family. CC {ECO:0000256|RuleBase:RU003630}. 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:KKR91733.1}. 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; LCAP01000002; KKR91733.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. DR Proteomes; UP000034190; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:InterPro. DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.50.1580; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00046; MurC; 1. DR HAMAP; MF_01963; MTAP; 1. DR InterPro; IPR010044; MTAP. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR018099; Purine_phosphorylase-2_CS. DR InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_murC. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; SSF53167; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01694; MTAP; 1. DR TIGRFAMs; TIGR01082; murC; 1. DR PROSITE; PS01240; PNP_MTAP_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU003630, KW ECO:0000256|SAAS:SAAS00459234}; KW Cell cycle {ECO:0000256|SAAS:SAAS00459266}; KW Cell division {ECO:0000256|SAAS:SAAS00459376}; KW Cell shape {ECO:0000256|SAAS:SAAS00459316}; KW Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00459280}; KW Complete proteome {ECO:0000313|Proteomes:UP000034190}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00459252}; KW Ligase {ECO:0000256|RuleBase:RU003630, ECO:0000256|SAAS:SAAS00459220, KW ECO:0000313|EMBL:KKR91733.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003630, KW ECO:0000256|SAAS:SAAS00459312}; KW Peptidoglycan synthesis {ECO:0000256|SAAS:SAAS00459348}; KW Reference proteome {ECO:0000313|Proteomes:UP000034190}. FT DOMAIN 12 250 PNP_UDP_1. {ECO:0000259|Pfam:PF01048}. FT DOMAIN 295 396 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 400 591 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 612 693 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. SQ SEQUENCE 771 AA; 86035 MW; 0B4D3664D4676934 CRC64; MNNNLINMNK IKIAIIGGSG LDDPGILKNA KKVNLATPFG ATAAPLICGQ IDGVDMVVLA RHGINHTFMP TKVPYRANIW ALKEIGCTHI IATTACGSLQ EKIKPRDLIF LDQFIDFTKH RNLTFFEDKV VHTAMADPFC PDLREILIKT AEELKFAHHK QGTIITIEGP RFSTRAESRF FKQMGADVIN MSTVPEVILA REVGICYGSV AMATDYDAWR KDEKAVTWGM VMQVMKDNTN NVVKLLLNII PKIALELADE ECENCGYIRS EKITNCKPPP NRFYIYMDLN KIKKIYLIGI KGVGMTMLAQ YLVGQNIDVS GSDGPEKYMT DAVLKKCGIK IIEKFDAKNI PHDADLIIYS TAYNAETNVE VAVALAGKIK IMTYAQALGE TFNQKYGIAV VGSHGKTTTT AWLGYVMKMS GLGPSVMAGA PVPQFDGCSI SGQADYLVIE ADEYQNKLQY YQPKAVLLNN IDYDHPDFFP TATDYENTYI EFIKKIPAKG FLVANFDDSL IRKIAQVNCR GKVITYAIDE TADYVAFDLK ANNGKQYFKV KLEVEDELDE EETRVEELGG FSIQLAGRHN ILNALAVIAT AIELNIELFK IRKYLAEFTG TARRMQALGE FRGATVIDDY AHHPTEIKAT VSAVRQKYGS RKLMVAFQPH TFSRTKALFN DFVKSFAQVD ELIILDIYGS AREKPGGAHS RDLAEKIRIR NQESLRRQGF GGQAGIRQTV KYISTLAECE RYLRDRVERN DVVVLMGAGD IFRVGENLVK G //