ID MURC_DEIRA Reviewed; 482 AA.
AC Q9RWN9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 138.
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};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046};
GN Name=murC {ECO:0000255|HAMAP-Rule:MF_00046}; OrderedLocusNames=DR_0627;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC
RC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.
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 -!- 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; AE000513; AAF10205.1; -; Genomic_DNA.
DR PIR; H75496; H75496.
DR RefSeq; NP_294350.1; NC_001263.1.
DR RefSeq; WP_010887272.1; NZ_JMLF01000001.1.
DR AlphaFoldDB; Q9RWN9; -.
DR SMR; Q9RWN9; -.
DR STRING; 243230.DR_0627; -.
DR PaxDb; 243230-DR_0627; -.
DR EnsemblBacteria; AAF10205; AAF10205; DR_0627.
DR GeneID; 69516873; -.
DR KEGG; dra:DR_0627; -.
DR PATRIC; fig|243230.17.peg.806; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_2_2_0; -.
DR InParanoid; Q9RWN9; -.
DR OrthoDB; 9804126at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002524; Chromosome I.
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 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..482
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000182086"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ SEQUENCE 482 AA; 50471 MW; AA4498FE81552755 CRC64;
MPQLPMTDSA PLPTPAPSSP AQPSAQPSLH YHLLGIGGIG MSAFARLLAT RGHRVSGCDQ
NLGAQTAGLE AQGIPVAAGH AAAHVTEEPF GKIDVLVASE AVPKSHPELA AARAAGVEVR
PRMALLGELL AAGPSVGVIG THGKTTTTSM IAVAMYGAGL DPSAFVGGNV PEFGGNARTG
TGPFVAEVDE SDRGFALLGC ETAVFTNAED DHVGGELATY WSTVEEQHAG FARFVAQSGR
VLFCADWPGL DTLCSGAREQ LTYGQSAGAD YRAVNVRPDE SGTTFDVEFR GERLGEARVS
LPGTHNVLNG LAALAVTHLY GGDFDRAARA LADFHGPGRR WEIKGERGGA LVVDDYAHNA
TKVASAVQAA RQTGRRVRVV FQPHRYLRTQ QSWPRLADAL MDADEVLVLD IAAASETPIE
GVHATLITDR MTQGGHPNVH YCPDRAAVVR DLRESAQPGD IIVTMGAGDV YRIAEEVVGG
SA
//
