ID MPL_ECOLI Reviewed; 457 AA.
AC P37773; P76804; Q2M673;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 24-JAN-2024, entry version 177.
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, ECO:0000269|PubMed:17384195};
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, ECO:0000303|PubMed:8808921};
GN Synonyms=yjfG; OrderedLocusNames=b4233, JW4192;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RX PubMed=2843822; DOI=10.1093/nar/16.17.8707;
RA Hamilton W.D.O., Harrison D.A., Dyer T.A.;
RT "Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene.";
RL Nucleic Acids Res. 16:8707-8707(1988).
RN [5]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND CHARACTERIZATION.
RC STRAIN=K12 / K10;
RX PubMed=8808921; DOI=10.1128/jb.178.18.5347-5352.1996;
RA Mengin-Lecreulx D., van Heijenoort J., Park J.T.;
RT "Identification of the mpl gene encoding UDP-N-acetylmuramate: L-alanyl-
RT gamma-D-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its
RT role in recycling of cell wall peptidoglycan.";
RL J. Bacteriol. 178:5347-5352(1996).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP DISRUPTION PHENOTYPE, AND SUBSTRATE SPECIFICITY.
RX PubMed=17384195; DOI=10.1128/jb.00087-07;
RA Herve M., Boniface A., Gobec S., Blanot D., Mengin-Lecreulx D.;
RT "Biochemical characterization and physiological properties of Escherichia
RT coli UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
RT ligase.";
RL J. Bacteriol. 189:3987-3995(2007).
CC -!- FUNCTION: Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl-
CC meso-diaminopimelate by linking it to UDP-N-acetylmuramate. The enzyme
CC can also use the tetrapeptide L-alanyl-gamma-D-glutamyl-meso-2,6-
CC diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl-gamma-D-
CC glutamyl-meso-2,6-diaminoheptandioyl-D-alanyl-D-alanine in vivo and in
CC vitro. {ECO:0000269|PubMed:17384195, ECO:0000269|PubMed:8808921}.
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 ECO:0000269|PubMed:17384195};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02020,
CC ECO:0000269|PubMed:17384195};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for UDP-N-acetyl-alpha-D-muramate
CC {ECO:0000269|PubMed:17384195};
CC KM=0.19 mM for ATP {ECO:0000269|PubMed:17384195};
CC KM=0.1 mM for L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
CC {ECO:0000269|PubMed:17384195};
CC Vmax=5.8 umol/min/mg enzyme {ECO:0000269|PubMed:17384195};
CC Note=kcat is 290 min(-1). {ECO:0000269|PubMed:17384195};
CC pH dependence:
CC Optimum pH is 8.4. {ECO:0000269|PubMed:17384195};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000255|HAMAP-Rule:MF_02020, ECO:0000269|PubMed:8808921}.
CC -!- INTERACTION:
CC P37773; P37773: mpl; NbExp=2; IntAct=EBI-562735, EBI-562735;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DISRUPTION PHENOTYPE: Enzyme ligase activity totally absent. No effect
CC on growth. {ECO:0000269|PubMed:17384195, ECO:0000269|PubMed:8808921}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. Mpl subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02020, ECO:0000305}.
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DR EMBL; U14003; AAA97130.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77190.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78233.1; -; Genomic_DNA.
DR EMBL; X12545; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S56459; S56459.
DR RefSeq; NP_418654.1; NC_000913.3.
DR RefSeq; WP_001219813.1; NZ_LN832404.1.
DR AlphaFoldDB; P37773; -.
DR SMR; P37773; -.
DR BioGRID; 4259323; 197.
DR BioGRID; 853041; 3.
DR DIP; DIP-10246N; -.
DR IntAct; P37773; 7.
DR STRING; 511145.b4233; -.
DR jPOST; P37773; -.
DR PaxDb; 511145-b4233; -.
DR EnsemblBacteria; AAC77190; AAC77190; b4233.
DR GeneID; 948752; -.
DR KEGG; ecj:JW4192; -.
DR KEGG; eco:b4233; -.
DR PATRIC; fig|1411691.4.peg.2469; -.
DR EchoBASE; EB2335; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_0_1_6; -.
DR InParanoid; P37773; -.
DR OMA; SGIAWDH; -.
DR OrthoDB; 9804126at2; -.
DR PhylomeDB; P37773; -.
DR BioCyc; EcoCyc:EG12440-MONOMER; -.
DR BioCyc; MetaCyc:EG12440-MONOMER; -.
DR BRENDA; 6.3.2.45; 2026.
DR UniPathway; UPA00544; -.
DR PRO; PR:P37773; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106418; F:UDP-N-acetylmuramate-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase activity; IDA:EcoCyc.
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; IMP:EcoCyc.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Ligase; Magnesium; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome; Secreted.
FT CHAIN 1..457
FT /note="UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-
FT meso-2,6-diaminoheptandioate ligase"
FT /id="PRO_0000101708"
FT BINDING 110..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02020"
SQ SEQUENCE 457 AA; 49874 MW; 105383EA5B696844 CRC64;
MRIHILGICG TFMGGLAMLA RQLGHEVTGS DANVYPPMST LLEKQGIELI QGYDASQLEP
QPDLVIIGNA MTRGNPCVEA VLEKNIPYMS GPQWLHDFVL RDRWVLAVAG THGKTTTAGM
ATWILEQCGY KPGFVIGGVP GNFEVSAHLG ESDFFVIEAD EYDCAFFDKR SKFVHYCPRT
LILNNLEFDH ADIFDDLKAI QKQFHHLVRI VPGQGRIIWP ENDINLKQTM AMGCWSEQEL
VGEQGHWQAK KLTTDASEWE VLLDGEKVGE VKWSLVGEHN MHNGLMAIAA ARHVGVAPAD
AANALGSFIN ARRRLELRGE ANGVTVYDDF AHHPTAILAT LAALRGKVGG TARIIAVLEP
RSNTMKMGIC KDDLAPSLGR ADEVFLLQPA HIPWQVAEVA EACVQPAHWS GDVDTLADMV
VKTAQPGDHI LVMSNGGFGG IHQKLLDGLA KKAEAAQ
//
