MURC_CORGL
ID MURC_CORGL Reviewed; 486 AA.
AC P94335; Q9L4H2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 5.
DT 03-AUG-2022, entry version 145.
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};
GN OrderedLocusNames=Cgl2157, cg2368;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MJ233;
RX PubMed=10091329; DOI=10.1007/s002530051385;
RA Wachi M., Wijayarathna C.D., Teraoka H., Nagai K.;
RT "A murC gene from coryneform bacteria.";
RL Appl. Microbiol. Biotechnol. 51:223-228(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RA Ramos A., Honrubia P., Gil J.A.;
RT "Characterization and chromosomal organization of the murD-murC region of
RT Brevibacterium lactofermentum ATCC 13869.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 397-486.
RX PubMed=9240446; DOI=10.1006/bbrc.1997.6930;
RA Kobayashi M., Asai Y., Hatakeyama K., Kijima N., Wachi M., Nagai K.,
RA Yukawa H.;
RT "Cloning, sequencing, and characterization of the ftsZ gene from coryneform
RT bacteria.";
RL Biochem. Biophys. Res. Commun. 236:383-388(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 400-486.
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=9738885; DOI=10.1007/s004380050793;
RA Honrubia M.P., Fernandez F.J., Gil J.A.;
RT "Identification, characterization, and chromosomal organization of the ftsZ
RT gene from Brevibacterium lactofermentum.";
RL Mol. Gen. Genet. 259:97-104(1998).
CC -!- FUNCTION: Cell wall formation.
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; AB015023; BAA34293.1; -; Genomic_DNA.
DR EMBL; AJ242646; CAB66325.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99550.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20497.1; -; Genomic_DNA.
DR EMBL; AB003132; BAA21685.1; -; Genomic_DNA.
DR EMBL; Y08964; CAA70160.1; -; Genomic_DNA.
DR RefSeq; NP_601359.1; NC_003450.3.
DR AlphaFoldDB; P94335; -.
DR SMR; P94335; -.
DR STRING; 196627.cg2368; -.
DR KEGG; cgb:cg2368; -.
DR KEGG; cgl:Cgl2157; -.
DR PATRIC; fig|196627.13.peg.2095; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_2_2_11; -.
DR OMA; DITYQLR; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000582; 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; IDA:CACAO.
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_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 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 TIGRFAMs; TIGR01082; murC; 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..486
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000182084"
FT BINDING 126..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
FT CONFLICT 255
FT /note="A -> R (in Ref. 2; CAB66325)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="I -> V (in Ref. 2; CAB66325)"
FT /evidence="ECO:0000305"
FT CONFLICT 369..372
FT /note="SAAR -> RRCA (in Ref. 2; CAB66325)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="I -> M (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="E -> G (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 51181 MW; 1F10D42136FFF72A CRC64;
MTTPHLDSAQ DIDLSRVHLI GIGGAGMSGV ARILLARGKT VTGSDAKDSR TLLPLRAVGA
TIAVGHAAEN LELSGELPTV VVTSFAAIPQ DNPELVRARE EGIPVIRRSD LLGELLEGST
QVLIAGTHGK TSTTSMSVVA MQAAGMDPSF AIGGQLNKAG TNAHHGTGEV FIAEADESDA
SLLRYKPNVA VVTNVEPDHL DFFKTPEAYF QVFDDFAGRI TPNGKLVVCL NDPHAAELGE
RSVRKGIKTV GYGTADAVQA HPEVPAMATI VDSQVVAEGT RATINIDGQE VSVILQIPGD
HMVLNGAAAL LAGYLVGGDV DKLVEGLSDF SGVRRRFEFH GAIEGGKFNG AAIYDDYAHH
PTEVTAVLSA ARTRVKAAGK GRVIVAFQPH LYSRTIEFQK EFAEALSLAD AAVVLEIYGA
REQPVDGVSS EIITDAMTIP VVYEPNFSAV PERIAEIAGP NDIVLTMGAG SVTMLAPEIL
DQLQNN
