MURC_NITMU
ID MURC_NITMU Reviewed; 493 AA.
AC Q2Y639;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=Nmul_A2493;
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB75782.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000103; ABB75782.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041352622.1; NZ_FNVK01000005.1.
DR AlphaFoldDB; Q2Y639; -.
DR SMR; Q2Y639; -.
DR STRING; 323848.Nmul_A2493; -.
DR PRIDE; Q2Y639; -.
DR EnsemblBacteria; ABB75782; ABB75782; Nmul_A2493.
DR KEGG; nmu:Nmul_A2493; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_2_2_4; -.
DR OrthoDB; 307881at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002718; 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; 3.40.1190.10; -; 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..493
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000242569"
FT BINDING 112..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ SEQUENCE 493 AA; 53116 MW; A905FAE14BEEA230 CRC64;
MKHKVKHIHF VGIGGSGMSG IAEVMLNLGY KISGSDIHDS VTTRRLKKLG ATVYIGHART
HVESADAVVT STAILPDNPE VLAARESKVP VVPRAIMLAE LLRLRQGIAI AGTHGKTTTT
SLITSVLAEA GMDPTFVIGG RLEAAGSHAK LGRGEFIVVE ADESDASFLH LQPVLAVVTN
IDADHMDTYE HDFGKLKQAF VDFVQHLPFY GMAVLCVDDA HVLEIMPAIT KPVTTYGLSE
TAQVRAADIR HSEGQMHFTA LIGVNGKTRK LKIVLNLPGL HNVQNALAAI AVCNEVGLPD
VSIVRALADF KGVDRRFQRY GEIPLTDPET GRNGSFTLID DYGHHPVEMA ATIAAARGAF
PGRRLVLAFQ PHRYTRTRDL FEDFVKVLST ADVLLLTEVY SAGEAPIIAA DSKSLARSLR
VLGKVEPIFV ERVDELEEAI HSIARDKDVV LVMGAGSVGG VAPTLSRDSQ VEARLLVSPK
ENREPAVLLL QGS