ID A0A0E3V5R4_9BACT Unreviewed; 441 AA. AC A0A0E3V5R4; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 29-SEP-2021, entry version 29. 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, RC ECO:0000313|Proteomes:UP000033054}; 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 bacterium RT isolated from gamma ray-irradiated soil."; RL Curr. Microbiol. 69:286-291(2014). CC -!- FUNCTION: Involved in cell wall formation. Catalyzes the final step in CC the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of CC murein. {ECO:0000256|HAMAP-Rule:MF_02019, CC ECO:0000256|RuleBase:RU004136}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L- CC alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl- CC meso-2,6-diaminopimeloyl-D-alanyl-D-alanine; Xref=Rhea:RHEA:28374, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57822, ChEBI:CHEBI:61386, ChEBI:CHEBI:83905, CC ChEBI:CHEBI:456216; EC=6.3.2.10; Evidence={ECO:0000256|HAMAP- CC Rule:MF_02019, 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 EnsemblBacteria; AKD53881; AKD53881; SD10_02150. DR KEGG; srd:SD10_02150; -. DR PATRIC; fig|1379870.5.peg.482; -. DR HOGENOM; CLU_031507_1_2_10; -. DR OrthoDB; 1861122at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000033054; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_02019; MurF; 1. DR InterPro; IPR036565; Mur-like_cat_sf. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR036615; Mur_ligase_C_dom_sf. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR035911; MurE/MurF_N. DR InterPro; IPR005863; UDP-N-AcMur_synth. 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 Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP- KW Rule:MF_02019}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_02019}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_02019}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_02019}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02019}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_02019}; Reference proteome {ECO:0000313|Proteomes:UP000033054}. FT DOMAIN 17..65 FT /note="Mur_ligase" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 99..289 FT /note="Mur_ligase_M" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 312..387 FT /note="Mur_ligase_C" FT /evidence="ECO:0000259|Pfam:PF02875" FT NP_BIND 100..106 FT /note="ATP" FT /evidence="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 //