MURC_WOLTR
ID MURC_WOLTR Reviewed; 536 AA.
AC Q5GTG5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
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=Wbm0118;
OS Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=292805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRS;
RX PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA Koonin E., Slatko B.;
RT "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT human pathogenic nematode.";
RL PLoS Biol. 3:599-614(2005).
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=AAW70709.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017321; AAW70709.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041571373.1; NC_006833.1.
DR AlphaFoldDB; Q5GTG5; -.
DR SMR; Q5GTG5; -.
DR STRING; 292805.Wbm0118; -.
DR EnsemblBacteria; AAW70709; AAW70709; Wbm0118.
DR KEGG; wbm:Wbm0118; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_2_2_5; -.
DR OrthoDB; 307881at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000534; 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.
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.
FT CHAIN 1..536
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000242615"
FT BINDING 133..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ SEQUENCE 536 AA; 58478 MW; A66FD8B8D812A8E1 CRC64;
MRILNYTIIN LVISKSLLLN MNGIKKGIIH IIGIGGIGMS AIAEILHNSN YKVQGSDAQS
NNNVDRLQKL GIEIYIGHNA NNIKQAQVVV YSSAIKSDNV ELVAARNNNK TILHRSGILA
EIMKDKYVIA VSGSSGKTTT TAMIASIFDH SNTDATVIVG GILNSYQNNS KLGKSDILLI
EADESDETML KIPANIAVIT SINNDHIDHY GTFDNIKNAF SQFINSADFA ILPDSVGIND
SESVSIKFGF EGVYPFVIQS PFVVPVHDIG IKKKKSASCS IKASNVKANN IRQHNNSIEF
DVLIDGCSID RSHWIPASCT ETTAVLPLSS TQITSLRSRI IKNVVLSNAI GMHKVSNALA
AISVAIKLGI NDVDIKKGLL EFKGVARRFS LVADIKDVKL IEDYAHHPSE IQATLTAARS
ITKGKIIGII EPFRFARIRN FFDEFIRIFM MFDYVILVPV HPPEDKPILG CRIDDIQEAL
ISNGFNNVKI MNDALLISNF ISDSTNSGDI VLFIGAGINV ARLARETVVF MSGVEI