ID MURC_ECOLI Reviewed; 491 AA.
AC P17952; O07099;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 27-MAR-2024, entry version 201.
DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase;
DE EC=6.3.2.8;
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase;
GN Name=murC; OrderedLocusNames=b0091, JW0089;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2197603; DOI=10.1093/nar/18.13.4014;
RA Ikeda M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.;
RT "Nucleotide sequence involving murG and murC in the mra gene cluster region
RT of Escherichia coli.";
RL Nucleic Acids Res. 18:4014-4014(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (MUTANT MURC3).
RC STRAIN=CGSC 5988;
RX PubMed=9166795; DOI=10.1021/bi9701078;
RA Eveland S.S., Pompliano D.L., Anderson M.S.;
RT "Conditionally lethal Escherichia coli murein mutants contain point defects
RT that map to regions conserved among murein and folyl poly-gamma-glutamate
RT ligases: identification of a ligase superfamily.";
RL Biochemistry 36:6223-6229(1997).
RN [6]
RP PROTEIN SEQUENCE OF 1-14, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX PubMed=7601127; DOI=10.1111/j.1432-1033.1995.0080i.x;
RA Liger D., Masson A., Blanot D., van Heijenoort J., Parquet C.;
RT "Over-production, purification and properties of the uridine-diphosphate-N-
RT acetylmuramate:L-alanine ligase from Escherichia coli.";
RL Eur. J. Biochem. 230:80-87(1995).
CC -!- FUNCTION: Cell wall formation. {ECO:0000269|PubMed:7601127}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) +
CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
CC Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
CC Evidence={ECO:0000269|PubMed:7601127};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for UDP-N-acetyl-alpha-D-muramate
CC {ECO:0000269|PubMed:7601127};
CC KM=20 uM for L-alanine {ECO:0000269|PubMed:7601127};
CC KM=450 uM for ATP {ECO:0000269|PubMed:7601127};
CC Vmax=17.3 umol/min/mg enzyme {ECO:0000269|PubMed:7601127};
CC pH dependence:
CC Optimum pH is 8.6. {ECO:0000269|PubMed:7601127};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:7601127};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- INTERACTION:
CC P17952; P77609: flxA; NbExp=3; IntAct=EBI-554607, EBI-553024;
CC P17952; P39328: ytfT; NbExp=3; IntAct=EBI-554607, EBI-554774;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}.
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DR EMBL; X52644; CAA36868.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38868.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73202.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96659.1; -; Genomic_DNA.
DR EMBL; U67892; AAB60787.1; -; Genomic_DNA.
DR PIR; JQ0545; CEECAM.
DR RefSeq; NP_414633.1; NC_000913.3.
DR RefSeq; WP_001096049.1; NZ_SSZK01000004.1.
DR PDB; 2F00; X-ray; 2.50 A; A/B=1-491.
DR PDBsum; 2F00; -.
DR AlphaFoldDB; P17952; -.
DR SMR; P17952; -.
DR BioGRID; 4261857; 473.
DR BioGRID; 850513; 5.
DR DIP; DIP-10278N; -.
DR IntAct; P17952; 16.
DR STRING; 511145.b0091; -.
DR BindingDB; P17952; -.
DR ChEMBL; CHEMBL5168; -.
DR jPOST; P17952; -.
DR PaxDb; 511145-b0091; -.
DR EnsemblBacteria; AAC73202; AAC73202; b0091.
DR GeneID; 75202092; -.
DR GeneID; 946153; -.
DR KEGG; ecj:JW0089; -.
DR KEGG; eco:b0091; -.
DR PATRIC; fig|511145.12.peg.95; -.
DR EchoBASE; EB0614; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_2_2_6; -.
DR InParanoid; P17952; -.
DR OMA; ELMRMKY; -.
DR OrthoDB; 9804126at2; -.
DR PhylomeDB; P17952; -.
DR BioCyc; EcoCyc:UDP-NACMUR-ALA-LIG-MONOMER; -.
DR BioCyc; MetaCyc:UDP-NACMUR-ALA-LIG-MONOMER; -.
DR BRENDA; 6.3.2.8; 2026.
DR SABIO-RK; P17952; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P17952; -.
DR PRO; PR:P17952; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IDA:EcoliWiki.
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; 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_00046; MurC; 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; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
DR NCBIfam; TIGR01082; murC; 1.
DR PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 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 3D-structure; ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Direct protein sequencing;
KW Ligase; Nucleotide-binding; Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..491
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000182089"
FT BINDING 126..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 344
FT /note="G->D: In murC3."
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:2F00"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2F00"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2F00"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 291..307
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 327..341
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 343..351
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:2F00"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 391..398
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:2F00"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:2F00"
FT HELIX 468..477
FT /evidence="ECO:0007829|PDB:2F00"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:2F00"
SQ SEQUENCE 491 AA; 53626 MW; D201B35931C013FB CRC64;
MNTQQLAKLR SIVPEMRRVR HIHFVGIGGA GMGGIAEVLA NEGYQISGSD LAPNPVTQQL
MNLGATIYFN HRPENVRDAS VVVVSSAISA DNPEIVAAHE ARIPVIRRAE MLAELMRFRH
GIAIAGTHGK TTTTAMVSSI YAEAGLDPTF VNGGLVKAAG VHARLGHGRY LIAEADESDA
SFLHLQPMVA IVTNIEADHM DTYQGDFENL KQTFINFLHN LPFYGRAVMC VDDPVIRELL
PRVGRQTTTY GFSEDADVRV EDYQQIGPQG HFTLLRQDKE PMRVTLNAPG RHNALNAAAA
VAVATEEGID DEAILRALES FQGTGRRFDF LGEFPLEPVN GKSGTAMLVD DYGHHPTEVD
ATIKAARAGW PDKNLVMLFQ PHRFTRTRDL YDDFANVLTQ VDTLLMLEVY PAGEAPIPGA
DSRSLCRTIR GRGKIDPILV PDPARVAEML APVLTGNDLI LVQGAGNIGK IARSLAEIKL
KPQTPEEEQH D
//
