MPL_HAEIN
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 03-AUG-2022, entry version 134.
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; Proteobacteria; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; L42023; AAC21795.1; -; Genomic_DNA.
DR PIR; B64002; B64002.
DR RefSeq; NP_438293.1; NC_000907.1.
DR RefSeq; WP_005694412.1; 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 OMA; SGIAWDH; -.
DR PhylomeDB; P43948; -.
DR BioCyc; HINF71421:G1GJ1-131-MON; -.
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; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 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 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 TIGRFAMs; TIGR01081; mpl; 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
