ID A0A0E3V5R4_9BACT Unreviewed; 441 AA. AC A0A0E3V5R4; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 08-JUN-2016, entry version 10. DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}; DE EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}; DE AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019}; GN Name=murF {ECO:0000256|HAMAP-Rule:MF_02019}; GN ORFNames=SD10_02150 {ECO:0000313|EMBL:AKD53881.1}; OS Spirosoma radiotolerans. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Spirosoma. OX NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD53881.1, ECO:0000313|Proteomes:UP000033054}; RN [1] {ECO:0000313|EMBL:AKD53881.1, ECO:0000313|Proteomes:UP000033054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG5A {ECO:0000313|EMBL:AKD53881.1}; RX PubMed=24748440; DOI=10.1007/s00284-014-0584-x; RA Lee J.J., Srinivasan S., Lim S., Joe M., Im S., Bae S.I., Park K.R., RA Han J.H., Park S.H., Joo B.M., Park S.J., Kim M.K.; RT "Spirosoma radiotolerans sp. nov., a gamma-radiation-resistant RT bacterium isolated from gamma ray-irradiated soil."; RL Curr. Microbiol. 69:286-291(2014). CC -!- FUNCTION: Involved in cell wall formation. Catalyzes the final CC step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the CC precursor of murein. {ECO:0000256|HAMAP-Rule:MF_02019, CC ECO:0000256|RuleBase:RU004136}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D- CC glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N- CC acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D- CC alanine. {ECO:0000256|HAMAP-Rule:MF_02019, CC ECO:0000256|RuleBase:RU004136}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019, CC ECO:0000256|RuleBase:RU004136}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily. CC {ECO:0000256|HAMAP-Rule:MF_02019}. 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; CP010429; AKD53881.1; -; Genomic_DNA. DR RefSeq; WP_046375476.1; NZ_CP010429.1. DR EnsemblBacteria; AKD53881; AKD53881; SD10_02150. DR KEGG; srd:SD10_02150; -. DR KO; K01929; -. DR Proteomes; UP000033054; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-HAMAP. 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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.1390.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_02019; MurF; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR005863; UDP-N-AcMur_synth. DR PANTHER; PTHR23135:SF3; PTHR23135:SF3; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR SUPFAM; SSF63418; SSF63418; 1. DR TIGRFAMs; TIGR01143; murF; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU003630}; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Complete proteome {ECO:0000313|Proteomes:UP000033054}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU003630, ECO:0000313|EMBL:AKD53881.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU003630}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}. FT DOMAIN 17 65 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 99 289 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 312 387 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT NP_BIND 100 106 ATP. {ECO:0000256|HAMAP-Rule:MF_02019}. SQ SEQUENCE 441 AA; 48176 MW; AABD08FCD6935727 CRC64; MMVTIEQLYH KFQECAGVST DTRRITPDCL FVALKGDTFD GNKFAEQALA AGARYAVVDD PEVASRVAGC LLVADGLTAL QGLARHHRQT FTFPVIALTG SNGKTTTKEL IAAVLSKNYQ LYATVGNLNN HIGVPLTLLA LNEQHELAIV EMGANHQKEI ELLCSIAQPT HGLITNVGKA HLEGFGGIEG VRKGKGELYD YLAQNAKTVF INSRDKTLTA MYRERLKAIR SETSFAEVIF YPAAESDQEP ITLLSESPVV VYRDSSGHDV TTHLPGRYNF ENMLAALAIG AYFGVSSDDV NRAVADYNPT NNRSQHITKG TNTVLLDAYN ANPSSMAAAI QQFAATPAKR KVVILGDMYE LGPESEAEHT ALGKLIAESK FDLVILAGKD MHYALGYLPK AYYFPDKFSL HNWLMDNPMT DTHILVKGSR GMSLESVVPF L //