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UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase (EC 6.3.2.10) (D-alanyl-D-alanine-adding enzyme) (UDP-MurNAc-pentapeptide synthetase)

 MURF_STRTO              Reviewed;         446 AA.
O33804;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
17-JAN-2003, sequence version 2.
28-FEB-2018, entry version 96.
RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02019};
EC=6.3.2.10 {ECO:0000255|HAMAP-Rule:MF_02019};
AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000255|HAMAP-Rule:MF_02019};
AltName: Full=UDP-MurNAc-pentapeptide synthetase;
Name=murF {ECO:0000255|HAMAP-Rule:MF_02019}; Synonyms=murX;
Streptomyces toyocaensis.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=55952;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NRRL 15009;
PubMed=9177243; DOI=10.1073/pnas.94.12.6480;
Marshall C.G., Broadhead G., Leskiw B.K., Wright G.D.;
"D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms
are highly homologous to the enterococcal vancomycin-resistance
ligases VanA and VanB.";
Proc. Natl. Acad. Sci. U.S.A. 94:6480-6483(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 40-43;
125-126; 190; 254-256; 311-341; 397 AND 408.
STRAIN=NRRL 15009;
PubMed=12060705; DOI=10.1073/pnas.102285099;
Pootoolal J., Thomas M.G., Marshall C.G., Neu J.M., Hubbard B.K.,
Walsh C.T., Wright G.D.;
"Assembling the glycopeptide antibiotic scaffold: the biosynthesis of
A47934 from Streptomyces toyocaensis NRRL15009.";
Proc. Natl. Acad. Sci. U.S.A. 99:8962-8967(2002).
-!- FUNCTION: Involved in cell wall formation. Catalyzes the final
step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the
precursor of murein. {ECO:0000255|HAMAP-Rule:MF_02019}.
-!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-
glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-
acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
alanine. {ECO:0000255|HAMAP-Rule:MF_02019}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_02019}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02019}.
-!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
{ECO:0000255|HAMAP-Rule:MF_02019}.
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EMBL; U82965; AAC23581.2; -; Genomic_DNA.
RefSeq; WP_037926351.1; NZ_JFCB01000001.1.
ProteinModelPortal; O33804; -.
SMR; O33804; -.
UniPathway; UPA00219; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.40.1190.10; -; 1.
Gene3D; 3.90.190.20; -; 1.
HAMAP; MF_02019; MurF; 1.
InterPro; IPR036565; Mur-like_cat_sf.
InterPro; IPR004101; Mur_ligase_C.
InterPro; IPR036615; Mur_ligase_C_dom_sf.
InterPro; IPR013221; Mur_ligase_cen.
InterPro; IPR000713; Mur_ligase_N.
InterPro; IPR035911; MurE/MurF_N.
InterPro; IPR005863; UDP-N-AcMur_synth.
Pfam; PF01225; Mur_ligase; 1.
Pfam; PF02875; Mur_ligase_C; 1.
Pfam; PF08245; Mur_ligase_M; 1.
SUPFAM; SSF53244; SSF53244; 1.
SUPFAM; SSF53623; SSF53623; 1.
SUPFAM; SSF63418; SSF63418; 1.
TIGRFAMs; TIGR01143; murF; 1.
3: Inferred from homology;
ATP-binding; Cell cycle; Cell division; Cell shape;
Cell wall biogenesis/degradation; Cytoplasm; Ligase;
Nucleotide-binding; Peptidoglycan synthesis.
CHAIN 1 446 UDP-N-acetylmuramoyl-tripeptide--D-
alanyl-D-alanine ligase.
/FTId=PRO_0000101705.
NP_BIND 108 114 ATP. {ECO:0000255}.
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


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