MURE_LACLA
ID MURE_LACLA Reviewed; 483 AA.
AC Q9CEN1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
DE EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_00208};
DE AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
GN Name=murE {ECO:0000255|HAMAP-Rule:MF_00208}; OrderedLocusNames=LL1806;
GN ORFNames=L53929;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Catalyzes the addition of an amino acid to the nucleotide
CC precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the
CC biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-
CC Rule:MF_00208}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00208}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}.
CC -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC consequently, for the gamma-phosphate positioning of ATP.
CC {ECO:0000255|HAMAP-Rule:MF_00208}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00208}.
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DR EMBL; AE005176; AAK05904.1; -; Genomic_DNA.
DR PIR; F86850; F86850.
DR RefSeq; NP_267963.1; NC_002662.1.
DR RefSeq; WP_003130330.1; NC_002662.1.
DR AlphaFoldDB; Q9CEN1; -.
DR SMR; Q9CEN1; -.
DR STRING; 272623.L53929; -.
DR PaxDb; Q9CEN1; -.
DR EnsemblBacteria; AAK05904; AAK05904; L53929.
DR KEGG; lla:L53929; -.
DR PATRIC; fig|272623.7.peg.1934; -.
DR eggNOG; COG0769; Bacteria.
DR HOGENOM; CLU_022291_4_2_9; -.
DR OMA; CFMEVSS; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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_00208; MurE; 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; IPR035911; MurE/MurF_N.
DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
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; TIGR01085; murE; 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..483
FT /note="UDP-N-acetylmuramyl-tripeptide synthetase"
FT /id="PRO_0000101904"
FT BINDING 43
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT BINDING 116..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT BINDING 160..161
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT BINDING 187
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT BINDING 195
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT MOD_RES 229
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
SQ SEQUENCE 483 AA; 53926 MW; 3F2D2F1A532E827C CRC64;
MIRLEQVIEI LKKDNNFREI SSAGEYYFNW PKEVNFDQLS YDSRKSTENT LFFAKGLNFK
KEYLTDLEAA FYVSEFDYEV ALPAIIVTDV KRAMALIAAS FYDFPQNKLK TLALTGTKGK
TTSAYFAKAI LDKMNGGKTA LLSTAQTTLD GKNYFKSELT TPESLDLLEM MAKALTNGMT
HLVMEVSSQA YKTERVYGLT FDVGVFLNIS PDHIGPVEHP TLEDYFYCKR QLLKNSRYFV
ANSEMNHFAI IKEELKERKI PHAFYGADSE NKIIESKGLH FVTDGSVSGA FDIRLLGRFN
QENALATALA TKALGASLEN IHDGLALAVV PGRMELLTAK NGAHIYIDYA HNGLSLENLV
EVVEEHHAGQ LVLVLGSTGN KGESRRKDFG QVIEKHPRLD VILTTDDSNR EDPKIIADEI
ASFVSRTLDF ELDRELAIKK AVSKTKSTDD AVIIAGKGTD MFQLKDGKRQ PYIGDTAAAQ
KYL
