MURF_BORBU
ID MURF_BORBU Reviewed; 464 AA.
AC Q44777; O51284;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 143.
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=BB_0304;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-464.
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA Dunn J.J., Butler-Loffredo L., Kieleczawa J., Medalle J., Luft B.J.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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; AE000783; AAC66644.1; -; Genomic_DNA.
DR EMBL; U43739; AAA85627.1; -; Genomic_DNA.
DR PIR; H70137; H70137.
DR RefSeq; NP_212438.1; NC_001318.1.
DR RefSeq; WP_010889724.1; NC_001318.1.
DR AlphaFoldDB; Q44777; -.
DR SMR; Q44777; -.
DR STRING; 224326.BB_0304; -.
DR EnsemblBacteria; AAC66644; AAC66644; BB_0304.
DR KEGG; bbu:BB_0304; -.
DR PATRIC; fig|224326.49.peg.703; -.
DR HOGENOM; CLU_031507_1_0_12; -.
DR OMA; VEMGANH; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001807; 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..464
FT /note="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
FT ligase"
FT /id="PRO_0000101695"
FT BINDING 125..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02019"
FT CONFLICT 462..464
FT /note="IFR -> YI (in Ref. 2; AAA85627)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 53446 MW; 29038B0C533799BC CRC64;
MRIKIKDILI SSKDVKFVGN IKNIERVVSF YSLDSREIKD DNINDSLYFA YKGNKVDGFS
FVKYLIDLGV KCFACSREHE SECIKYLNDN EGLVFLLTSN VIKLLQALAS FLIEKTSFKR
IAITGSNGKT TTKEMLYSIL SKKYKTYKTW GNLNSDIGLP LSILRVEGNE EYAVFEVGVS
YVGEMDLLSQ ILKPEIVIIT NISYAHMQAF KELQAIAFEK SKIIGKNIEI FVVNEMNDYC
VYLEKRAKIA NPNVKIVYFD FENLSIKSFS FLDGKFSFDF VYKGFEYSIL LLGRHNIFNA
IGCINLALFL GMREKEIKEG LIETAFQKGR AEILTKNGYL ILNDSYNGNM GSFMALKNMI
LDLNIQNKKF IVLGSFKELG ELAYKTHKDL IQEAISMNFD KIFLIGEEFL DVRDSENLVE
KCLYYFSEFD KFIDFFLKSL EPSVFIVIKG SRFNRLERIL NIFR
