ID A0A0G0VG87_9BACT Unreviewed; 815 AA.
AC A0A0G0VG87;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|HAMAP-Rule:MF_02209};
DE Includes:
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639};
DE EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639};
DE AltName: Full=D-glutamic acid-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00639};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000256|HAMAP-Rule:MF_00639};
DE Includes:
DE RecName: Full=UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate epimerase {ECO:0000256|HAMAP-Rule:MF_02209};
DE EC=5.1.1.23 {ECO:0000256|HAMAP-Rule:MF_02209};
DE AltName: Full=UDP-MurNAc-L-Ala-L-Glu epimerase {ECO:0000256|HAMAP-Rule:MF_02209};
GN Name=murD {ECO:0000256|HAMAP-Rule:MF_00639};
GN Synonyms=murL {ECO:0000256|HAMAP-Rule:MF_02209};
GN ORFNames=UU50_C0001G0048 {ECO:0000313|EMBL:KKR99989.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWC1_41_20.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618983 {ECO:0000313|EMBL:KKR99989.1, ECO:0000313|Proteomes:UP000033930};
RN [1] {ECO:0000313|EMBL:KKR99989.1, ECO:0000313|Proteomes:UP000033930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Cell wall formation. Catalyzes epimerization of the terminal
CC L-glutamate in UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate.
CC {ECO:0000256|HAMAP-Rule:MF_02209}.
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC {ECO:0000256|HAMAP-Rule:MF_00639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate
CC = AMP + diphosphate + H(+) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-
CC D-glutamate; Xref=Rhea:RHEA:58812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:83900, ChEBI:CHEBI:142725, ChEBI:CHEBI:456215;
CC EC=5.1.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_02209};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00639}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC Rule:MF_00639}.
CC -!- SIMILARITY: Belongs to the MurL family. {ECO:0000256|HAMAP-
CC Rule:MF_02209}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKR99989.1}.
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DR EMBL; LCAW01000001; KKR99989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0VG87; -.
DR PATRIC; fig|1618983.3.peg.47; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000033930; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IEA:UniProtKB-UniRule.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate 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; 2.
DR HAMAP; MF_00639; MurD; 1.
DR HAMAP; MF_02209; MurL; 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; IPR005762; MurD.
DR InterPro; IPR043689; MurL.
DR PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00639}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_02209};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00639};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00639}; Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639}.
FT DOMAIN 519..622
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 677..747
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 521..527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ SEQUENCE 815 AA; 92074 MW; 6D188C2234A89E92 CRC64;
MKPKSTVFEF KGYALNTKNK QITFDYSIAF SNQESLNFTE TIILPRLPKG VTQESLRVFL
EPLHLILGIS YYKLYCPPKI KLGFKLSKEQ AEFWHTVYKK GLGEFLYRNK LDPKIIAKFP
ASNIKPCPVL IPVQDRCLLG IGGGKDSIVA AELLKENKHD FSSFLVETQR QDPICEKVIK
TIGKPSIKIK RVLDPKLFEP HTDSYNGHIP ISAIFALLGL LSAALYDYRF VLVGNEYSSN
FGNLTYKGQT INHQWSKTSE FEAMLQDYTR KYITPDIVYT SALRQFYELR IAMMFAKYTK
YHHLFTSCNR SFKVHKERTH TLWCGECPKC AFTFLMLAPF LPKTELASTF GKNLLADESL
IPLYRDLLGM GNLKPFDCVG TFEESRAAFS MASDKYRKDA VVKKLLPSVK DGKKLQAQVL
RTVPAPTSPT QFRFLGIESV CILGFGKEGS VTQKYLKKFY PKIKVGVLDQ TTDKKYLEHQ
ANFDLAIKTP GIQKSKVTIP YVTATNLFFS SVKNLTIGVT GSKGKSTTAS LIYEMLKADG
RKVRLLGNIG NPMLASLLAK IDPAEIFVLE LSSYMLDDIE YSPNIAVLLN LFPEHMDYHG
GVDEYYKAKK QIFAFQTLGD IALRPEFKAK IPVSDKDIPL LGEHNRKNIK AAINVVKEIG
VSDSSIIEAI KKFKSLPHRL EEVGEFKGIK FIDDAISTTP ESTIEALRAL KNVKTIFLGG
EDRGYDFKEL ERELRSIGVE NIVLFPDTGK RILSSTKGLK ILKTKNMEIA VKFAYKVTPE
GSTCLLSTAS PSYSIWKNFE EKGDLFKKFV KKYSK
//
