MURF_MYCLE
ID MURF_MYCLE Reviewed; 517 AA.
AC O69556;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02019};
DE EC=6.3.2.10 {ECO:0000255|HAMAP-Rule:MF_02019};
DE AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000255|HAMAP-Rule:MF_02019};
DE AltName: Full=UDP-MurNAc-pentapeptide synthetase;
GN Name=murF {ECO:0000255|HAMAP-Rule:MF_02019}; OrderedLocusNames=ML0910;
GN ORFNames=MLCB268.06c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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}.
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};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02019}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02019}.
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DR EMBL; AL022602; CAA18672.1; -; Genomic_DNA.
DR EMBL; AL583920; CAC31291.1; -; Genomic_DNA.
DR PIR; H87022; H87022.
DR RefSeq; NP_301693.1; NC_002677.1.
DR RefSeq; WP_010908017.1; NC_002677.1.
DR AlphaFoldDB; O69556; -.
DR SMR; O69556; -.
DR STRING; 272631.ML0910; -.
DR EnsemblBacteria; CAC31291; CAC31291; CAC31291.
DR KEGG; mle:ML0910; -.
DR PATRIC; fig|272631.5.peg.1653; -.
DR Leproma; ML0910; -.
DR eggNOG; COG0770; Bacteria.
DR HOGENOM; CLU_031507_0_0_11; -.
DR OMA; VEMGANH; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine 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-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_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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..517
FT /note="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
FT ligase"
FT /id="PRO_0000101700"
FT BINDING 138..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02019"
SQ SEQUENCE 517 AA; 52874 MW; B503324330DD1FAD CRC64;
MIDLTVARVT EIVGGALVDI SPEEAAERRV TGSVEFDSRA VGPGGLFLAL PGARSDGHDH
AASAIAAGAV AVLAARPVGV PAIVVAPDPR TGDGGLTGVL EHDADGSGAA VLAALAKLAK
AVAAELVAGG LTIIGITGSS GKTSTKDLVA VVLELLGEVV APPESFNNEL GHPWTVLRAT
RSTDYLILEM SARRPGNIAA LAAIAPPKIG VVLNVGTAHL GEFGSREAIA RTKTELPQAI
MQSGVVILNV DDPAVAAMAD ATVARVIRVS RGSYSHPGSP NSPDVWTGPV SLDELARPRF
TLHTRDPRAG ATEIQLGVYG DHQVANALCA AAVGLECGAS VEEVAVALAA TGPVSRHRMQ
VTTRADGVTV IDDTYNANPD SMRAGLQALA WIAHGGTHDK NQPGSCARRS WAVLGEMAEL
GEDSITEHDR IGRLAVRLDV SRLVVVGGGR SINAMHRGAV MEGSWGLETV NVADPAAALT
LLRAEVRPGD VVLIKASHSV GLGALADVLV GDGAIRP
