ID MURC_STAA8 Reviewed; 437 AA.
AC Q2FXJ0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00046};
DE EC=6.3.2.8 {ECO:0000255|HAMAP-Rule:MF_00046, ECO:0000269|PubMed:20659527};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046};
GN Name=murC {ECO:0000255|HAMAP-Rule:MF_00046, ECO:0000303|PubMed:20659527};
GN OrderedLocusNames=SAOUHSC_01856;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NCTC 8325 / PS 47;
RX PubMed=20659527; DOI=10.1016/j.biochi.2010.07.009;
RA Patin D., Boniface A., Kovac A., Herve M., Dementin S., Barreteau H.,
RA Mengin-Lecreulx D., Blanot D.;
RT "Purification and biochemical characterization of Mur ligases from
RT Staphylococcus aureus.";
RL Biochimie 92:1793-1800(2010).
CC -!- FUNCTION: Cell wall formation (PubMed:20659527). Can also use L-serine
CC and glycine, but they are incorporated 4.3- and 7-fold less rapidly,
CC respectively, than L-alanine (PubMed:20659527).
CC {ECO:0000269|PubMed:20659527}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) +
CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
CC Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00046,
CC ECO:0000269|PubMed:20659527};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.28 mM for UDP-MurNAc {ECO:0000269|PubMed:20659527};
CC KM=0.44 mM for L-alanine {ECO:0000269|PubMed:20659527};
CC KM=2.0 mM for ATP {ECO:0000269|PubMed:20659527};
CC Vmax=2.9 umol/min/mg enzyme {ECO:0000269|PubMed:20659527};
CC pH dependence:
CC Optimum pH is 8.2-8.8. {ECO:0000269|PubMed:20659527};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00046}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC Rule:MF_00046}.
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DR EMBL; CP000253; ABD30922.1; -; Genomic_DNA.
DR RefSeq; WP_000150168.1; NZ_LS483365.1.
DR RefSeq; YP_500360.1; NC_007795.1.
DR AlphaFoldDB; Q2FXJ0; -.
DR SMR; Q2FXJ0; -.
DR STRING; 93061.SAOUHSC_01856; -.
DR PaxDb; 1280-SAXN108_1770; -.
DR GeneID; 3920534; -.
DR KEGG; sao:SAOUHSC_01856; -.
DR PATRIC; fig|93061.5.peg.1689; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_1_0_9; -.
DR OrthoDB; 9804126at2; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:Q2FXJ0; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; 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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00046; MurC; 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; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
DR NCBIfam; TIGR01082; murC; 1.
DR PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 1: Evidence at protein level;
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..437
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_1000004419"
FT BINDING 108..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ SEQUENCE 437 AA; 49188 MW; 335765DF79D87355 CRC64;
MTHYHFVGIK GSGMSSLAQI MHDLGHEVQG SDIENYVFTE VALRNKGIKI LPFDANNIKE
DMVVIQGNAF ASSHEEIVRA HQLKLDVVSY NDFLGQIIDQ YTSVAVTGAH GKTSTTGLLS
HVMNGDKKTS FLIGDGTGMG LPESDYFAFE ACEYRRHFLS YKPDYAIMTN IDFDHPDYFK
DINDVFDAFQ EMAHNVKKGI IAWGDDEHLR KIEADVPIYY YGFKDSDDIY AQNIQITDKG
TAFDVYVDGE FYDHFLSPQY GDHTVLNALA VIAISYLEKL DVTNIKEALE TFGGVKRRFN
ETTIANQVIV DDYAHHPREI SATIETARKK YPHKEVVAVF QPHTFSRTQA FLNEFAESLS
KADRVFLCEI FGSIRENTGA LTIQDLIDKI EGASLINEDS INVLEQFDNA VILFMGAGDI
QKLQNAYLDK LGMKNAF
//
