ID A0A3M0LPW0_9LACO Unreviewed; 455 AA. AC A0A3M0LPW0; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 07-APR-2021, 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=F5ESL0246_06610 {ECO:0000313|EMBL:RMC27609.1}; OS Lactobacillus sp. ESL0246. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus; unclassified Lactobacillus. OX NCBI_TaxID=2069359 {ECO:0000313|EMBL:RMC27609.1, ECO:0000313|Proteomes:UP000279155}; RN [1] {ECO:0000313|EMBL:RMC27609.1, ECO:0000313|Proteomes:UP000279155} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ESL0246 {ECO:0000313|EMBL:RMC27609.1, RC ECO:0000313|Proteomes:UP000279155}; RA Ellegaard K.M., Brochet S., Bonilla-Rosso G., Emery O., Glover N., RA Hadadi N., Jaron K.S., Van Der Meer J.R., Sentchilo V., Tagini F., RA Sage Class S., Engel P.; RT "Genomic changes underlying host specialization in the bee gut symbiont RT Lactobacillus Firm5."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. 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-L-lysine = ADP + H(+) + phosphate + UDP-N- CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D- CC alanine; Xref=Rhea:RHEA:16085, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57822, ChEBI:CHEBI:70758, CC ChEBI:CHEBI:83903, ChEBI:CHEBI:456216; EC=6.3.2.10; CC Evidence={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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RMC27609.1}. 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; REHC01000011; RMC27609.1; -; Genomic_DNA. DR EnsemblBacteria; RMC27609; RMC27609; F5ESL0246_06610. DR UniPathway; UPA00219; -. DR Proteomes; UP000279155; Unassembled WGS sequence. 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: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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_02019}; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_02019, ECO:0000256|RuleBase:RU004136}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000313|EMBL:RMC27609.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_02019, ECO:0000256|RuleBase:RU004136}. FT DOMAIN 24..85 FT /note="Mur_ligase" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 107..290 FT /note="Mur_ligase_M" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 325..391 FT /note="Mur_ligase_C" FT /evidence="ECO:0000259|Pfam:PF02875" FT NP_BIND 109..115 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02019" SQ SEQUENCE 455 AA; 50366 MW; 9E14A0353B8C8187 CRC64; MKMQLAEIAK AINSTCEGDD QTIITSVAFD SRKIVLGGLF VPLQGERDGH DFINSAINNG ASATLWEKGH PDKPTSIAVL EVEDPLDSMQ KLAQYYLNKV NPTVVGITGS NGKTTTKDMT AAVLAKRFNV HKTAANFNNE IGVPMTILEM KPNTEILVLE MGMDHSGQLH HLSELTHPDV TVITMIGEAH IEFLGSRAAI ADAKMEITDF LREDGELIYN GDEPLLCDRA QKIHQSMVTF GFAKTDSVYA TEFRSYKHHA SFMINDSDCK FTIPMIGKHN VSNALSALCV GKHFGEKDEE IAAALASFTP TANRMEWEKG DVGEDIMSDV YNSNPTAVRA VLASFGQIQI TPGSRRIAVL GDMLELGERS ADLHAQLVDC LDPQVINEVY LFGSEMKYLA DALKDRYGLE YLHYYPQDQM QHMIADLKND IKPHDIVVLK GSHGMHLEKV VERLR //