MURF_ECOLI
ID MURF_ECOLI Reviewed; 452 AA.
AC P11880; O07100; P77636;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000305};
DE EC=6.3.2.10 {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000269|PubMed:2186811};
DE AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000303|PubMed:2186811};
DE AltName: Full=UDP-MurNAc-pentapeptide synthetase {ECO:0000303|PubMed:2668880};
GN Name=murF {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000303|PubMed:2668880};
GN Synonyms=mra; OrderedLocusNames=b0086, JW0084;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2668880; DOI=10.1093/nar/17.13.5379;
RA Parquet C., Flouret B., Mengin-Lecreulx D., van Heijenoort J.;
RT "Nucleotide sequence of the murF gene encoding the UDP-MurNAc-pentapeptide
RT synthetase of Escherichia coli.";
RL Nucleic Acids Res. 17:5379-5379(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MB2884;
RX PubMed=8973200; DOI=10.1021/bi961872+;
RA Anderson M.S., Eveland S.S., Onishi H.R., Pompliano D.L.;
RT "Kinetic mechanism of the Escherichia coli UDPMurNAc-tripeptide D-alanyl-D-
RT alanine-adding enzyme: use of a glutathione S-transferase fusion.";
RL Biochemistry 35:16264-16269(1996).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 61
RP AND 178.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT MURF2.
RC STRAIN=CGSC 5990;
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 [7]
RP PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT,
RP AND SUBCELLULAR LOCATION.
RX PubMed=2186811; DOI=10.1021/bi00461a023;
RA Duncan K., van Heijenoort J., Walsh C.T.;
RT "Purification and characterization of the D-alanyl-D-alanine-adding enzyme
RT from Escherichia coli.";
RL Biochemistry 29:2379-2386(1990).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=11090285; DOI=10.1006/jmbi.2000.4215;
RA Yan Y., Munshi S., Leiting B., Anderson M.S., Chrzas J., Chen Z.;
RT "Crystal structure of Escherichia coli UDPMurNAc-tripeptide D-alanyl-D-
RT alanine-adding enzyme (MurF) at 2.3-A resolution.";
RL J. Mol. Biol. 304:435-445(2000).
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:0000255|HAMAP-Rule:MF_02019, ECO:0000269|PubMed:2186811}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-
CC alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) +
CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-
CC meso-2,6-diaminopimeloyl-D-alanyl-D-alanine; Xref=Rhea:RHEA:28374,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57822, ChEBI:CHEBI:61386, ChEBI:CHEBI:83905,
CC ChEBI:CHEBI:456216; EC=6.3.2.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02019, ECO:0000269|PubMed:2186811};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000269|PubMed:2186811}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2186811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02019,
CC ECO:0000269|PubMed:2186811}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000305}.
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DR EMBL; X15432; CAA33473.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38863.1; -; Genomic_DNA.
DR EMBL; U67891; AAC44657.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73197.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96654.2; -; Genomic_DNA.
DR EMBL; U67893; AAB60788.1; -; Genomic_DNA.
DR PIR; F64730; F64730.
DR RefSeq; NP_414628.1; NC_000913.3.
DR RefSeq; WP_000626685.1; NZ_LN832404.1.
DR PDB; 1GG4; X-ray; 2.30 A; A/B=1-452.
DR PDBsum; 1GG4; -.
DR AlphaFoldDB; P11880; -.
DR SMR; P11880; -.
DR BioGRID; 4261642; 419.
DR BioGRID; 849214; 1.
DR DIP; DIP-10281N; -.
DR IntAct; P11880; 11.
DR STRING; 511145.b0086; -.
DR BindingDB; P11880; -.
DR ChEMBL; CHEMBL2540; -.
DR jPOST; P11880; -.
DR PaxDb; P11880; -.
DR PRIDE; P11880; -.
DR EnsemblBacteria; AAC73197; AAC73197; b0086.
DR EnsemblBacteria; BAB96654; BAB96654; BAB96654.
DR GeneID; 944813; -.
DR KEGG; ecj:JW0084; -.
DR KEGG; eco:b0086; -.
DR PATRIC; fig|1411691.4.peg.2194; -.
DR EchoBASE; EB0617; -.
DR eggNOG; COG0770; Bacteria.
DR HOGENOM; CLU_031507_4_0_6; -.
DR InParanoid; P11880; -.
DR OMA; VEMGANH; -.
DR PhylomeDB; P11880; -.
DR BioCyc; EcoCyc:UDP-NACMURALGLDAPAALIG-MON; -.
DR BioCyc; MetaCyc:UDP-NACMURALGLDAPAALIG-MON; -.
DR BRENDA; 6.3.2.10; 2026.
DR BRENDA; 6.3.2.8; 2026.
DR SABIO-RK; P11880; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P11880; -.
DR PRO; PR:P11880; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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; IDA:EcoCyc.
DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine 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; IMP:EcoCyc.
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 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..452
FT /note="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
FT ligase"
FT /id="PRO_0000101698"
FT BINDING 107..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02019"
FT VARIANT 288
FT /note="A -> T (in murF2; temperature-sensitive mutant with
FT low activity)"
FT /evidence="ECO:0000269|PubMed:9166795"
FT CONFLICT 61
FT /note="G -> A (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="A -> R (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1GG4"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:1GG4"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 281..295
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 337..349
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 350..358
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 367..382
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 385..393
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 395..400
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 410..423
FT /evidence="ECO:0007829|PDB:1GG4"
FT STRAND 425..432
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:1GG4"
FT HELIX 440..446
FT /evidence="ECO:0007829|PDB:1GG4"
SQ SEQUENCE 452 AA; 47447 MW; B46E2E57BDBBC572 CRC64;
MISVTLSQLT DILNGELQGA DITLDAVTTD TRKLTPGCLF VALKGERFDA HDFADQAKAG
GAGALLVSRP LDIDLPQLIV KDTRLAFGEL AAWVRQQVPA RVVALTGSSG KTSVKEMTAA
ILSQCGNTLY TAGNLNNDIG VPMTLLRLTP EYDYAVIELG ANHQGEIAWT VSLTRPEAAL
VNNLAAAHLE GFGSLAGVAK AKGEIFSGLP ENGIAIMNAD NNDWLNWQSV IGSRKVWRFS
PNAANSDFTA TNIHVTSHGT EFTLQTPTGS VDVLLPLPGR HNIANALAAA ALSMSVGATL
DAIKAGLANL KAVPGRLFPI QLAENQLLLD DSYNANVGSM TAAVQVLAEM PGYRVLVVGD
MAELGAESEA CHVQVGEAAK AAGIDRVLSV GKQSHAISTA SGVGEHFADK TALITRLKLL
IAEQQVITIL VKGSRSAAME EVVRALQENG TC
