ID   MURF_STRTO              Reviewed;         446 AA.
AC   O33804;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   17-JAN-2003, sequence version 2.
DT   03-AUG-2022, entry version 108.
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}; Synonyms=murX;
OS   Streptomyces toyocaensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=55952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 15009;
RX   PubMed=9177243; DOI=10.1073/pnas.94.12.6480;
RA   Marshall C.G., Broadhead G., Leskiw B.K., Wright G.D.;
RT   "D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms are
RT   highly homologous to the enterococcal vancomycin-resistance ligases VanA
RT   and VanB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:6480-6483(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 40-43; 125-126;
RP   190; 254-256; 311-341; 397 AND 408.
RC   STRAIN=NRRL 15009;
RX   PubMed=12060705; DOI=10.1073/pnas.102285099;
RA   Pootoolal J., Thomas M.G., Marshall C.G., Neu J.M., Hubbard B.K.,
RA   Walsh C.T., Wright G.D.;
RT   "Assembling the glycopeptide antibiotic scaffold: the biosynthesis of
RT   A47934 from Streptomyces toyocaensis NRRL15009.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:8962-8967(2002).
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; U82965; AAC23581.2; -; Genomic_DNA.
DR   RefSeq; WP_037926351.1; NZ_JFCB01000001.1.
DR   AlphaFoldDB; O33804; -.
DR   SMR; O33804; -.
DR   STRING; 55952.BU52_01160; -.
DR   eggNOG; COG0770; Bacteria.
DR   OMA; TIINDAW; -.
DR   UniPathway; UPA00219; -.
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.
FT   CHAIN           1..446
FT                   /note="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
FT                   ligase"
FT                   /id="PRO_0000101705"
FT   BINDING         108..114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   446 AA;  44892 MW;  DE3636764FC46D5F CRC64;
     MIPLGLGEIA EIVGGKATGE SVTVTAPAVL DSRQAEPGGL FVAFAGEHAD GHDYAERAGR
     AGAVAVLGSR PTSLPTVVVE DVRTALQTLA AHVVARLRDG LTVVGVTGSQ GKTGTKDLLA
     AVLSGAGPTV ATTGSLNNEL GVPLTMLRAQ AATRFLVLEM GARHEGDIAE LTGLVAPDIA
     VVLNVGVAHL GEFGSRAAIA RAKGELVQGL VPGGTAVLNA DDPRVASMSV LTDGPVLTFG
     RTDPADVQVL DVVLDRLGRP SCTLRTVDTS ARLALPLVGA HQALNASAAA AAALAAGVPL
     DLATTALTTA SLSPWRMELR DLACGATLLN DSYNANPDST RAALDALSAI EGGRRIAVLG
     EMLELGDGSE AEHRAVGAYA AARADVVVAV GEAARPLADG AGERAVVLAG NDAAVDWLRD
     HLAAGDVVLV KASRGARLDE VAAGLA