ID MPL_HAEIN Reviewed; 453 AA. AC P43948; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 140. DE RecName: Full=UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase {ECO:0000255|HAMAP-Rule:MF_02020}; DE EC=6.3.2.45 {ECO:0000255|HAMAP-Rule:MF_02020}; DE AltName: Full=Murein peptide ligase {ECO:0000255|HAMAP-Rule:MF_02020}; DE AltName: Full=UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_02020}; GN Name=mpl {ECO:0000255|HAMAP-Rule:MF_02020}; OrderedLocusNames=HI_0121; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl- CC meso-diaminopimelate by linking it to UDP-N-acetylmuramate. CC {ECO:0000255|HAMAP-Rule:MF_02020}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate + CC UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N- CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6- CC diaminoheptanedioate; Xref=Rhea:RHEA:29563, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:61401, CC ChEBI:CHEBI:70757, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; CC EC=6.3.2.45; Evidence={ECO:0000255|HAMAP-Rule:MF_02020}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_02020}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000255|HAMAP-Rule:MF_02020}. CC -!- SIMILARITY: Belongs to the MurCDEF family. Mpl subfamily. CC {ECO:0000255|HAMAP-Rule:MF_02020}. 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; L42023; AAC21795.1; -; Genomic_DNA. DR PIR; B64002; B64002. DR RefSeq; NP_438293.1; NC_000907.1. DR AlphaFoldDB; P43948; -. DR SMR; P43948; -. DR STRING; 71421.HI_0121; -. DR DNASU; 951026; -. DR EnsemblBacteria; AAC21795; AAC21795; HI_0121. DR KEGG; hin:HI_0121; -. DR PATRIC; fig|71421.8.peg.125; -. DR eggNOG; COG0773; Bacteria. DR HOGENOM; CLU_028104_0_1_6; -. DR OrthoDB; 9804126at2; -. DR PhylomeDB; P43948; -. DR BioCyc; HINF71421:G1GJ1-131-MONOMER; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0106418; F:UDP-N-acetylmuramate-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate 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-KW. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1. DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_02020; Mpl; 1. DR InterPro; IPR005757; Mpl. 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 NCBIfam; TIGR01081; mpl; 1. DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1. DR PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF51984; MurCD N-terminal domain; 1. DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1. DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Ligase; Magnesium; Nucleotide-binding; KW Peptidoglycan synthesis; Reference proteome. FT CHAIN 1..453 FT /note="UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl- FT meso-2,6-diaminoheptandioate ligase" FT /id="PRO_0000101709" FT BINDING 111..117 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02020" SQ SEQUENCE 453 AA; 50074 MW; 5E7E71A07646EB7D CRC64; MKHIHILGIC GTFMGGVAMI AKQMGYHVTG SDTNVYPPMS TFLEEQGIEI IPNYDVAQLQ PAPDMVIVGN AMKRGNPCVE YVLENNLKYT SGPQWLHDHL LRDRWVLAVS GTHGKTTTTG MLTWVLEQNG LKSGFLIGGI AGNFGISARL GDSPYFIIEA DEYDTAFFDK RSKFVHYNPR TLIVNNISFD HADIFDDLKA IQRQFHHMIR TIPASGLVLS SASEQSAKET LALGCWSQQQ FLGKDNEWFA ERITNDASHF AVFHHGEKVA EVKWNVVGQH NMHNALMAIA AAHHTGVAIE DACKALGSFV NAKRRLEVKG EVNSITVYDD FAHHPEAILA TLTALRDKVG GGVRILAVLE PRSNTMKMGV HKDDIAPALG RADAVFMLQP EQLSWEVADI ANQCVQPAYW NANLDRLVDM IVAKAQPTDH ILVMSNGSFG GIHQKILDKL KLK //