MURD2_XYLFA
ID MURD2_XYLFA Reviewed; 468 AA.
AC Q9PEB0;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_02208};
DE EC=6.3.2.53 {ECO:0000255|HAMAP-Rule:MF_02208};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-L-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_02208};
DE Short=UDP-MurNAc-L-Ala-L-Glu synthetase {ECO:0000255|HAMAP-Rule:MF_02208};
GN Name=murD2 {ECO:0000255|HAMAP-Rule:MF_02208}; OrderedLocusNames=XF_1118;
OS Xylella fastidiosa (strain 9a5c).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=160492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c;
RX PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of L-glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine.
CC {ECO:0000255|HAMAP-Rule:MF_02208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-
CC glutamate; Xref=Rhea:RHEA:58816, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:142725, ChEBI:CHEBI:456216;
CC EC=6.3.2.53; Evidence={ECO:0000255|HAMAP-Rule:MF_02208};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02208}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02208}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurD2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02208}.
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DR EMBL; AE003849; AAF83928.1; -; Genomic_DNA.
DR PIR; C82722; C82722.
DR RefSeq; WP_010893635.1; NC_002488.3.
DR AlphaFoldDB; Q9PEB0; -.
DR SMR; Q9PEB0; -.
DR STRING; 160492.XF_1118; -.
DR EnsemblBacteria; AAF83928; AAF83928; XF_1118.
DR KEGG; xfa:XF_1118; -.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_032540_4_1_6; -.
DR OMA; KGMHNVE; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000812; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:InterPro.
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_00639; MurD; 1.
DR HAMAP; MF_02208; MurD2_subfam; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR005762; MurD.
DR InterPro; IPR043687; MurD2.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01087; murD; 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..468
FT /note="UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase"
FT /id="PRO_0000109130"
FT BINDING 122..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02208"
SQ SEQUENCE 468 AA; 49502 MW; 6B9296E90C8A7375 CRC64;
MRISALEGCR VALWGWGRES RAAYRTFRAA FPKQPLTLFC TIAEATEVQA LADPVLSIET
EVSVPRLAAF DVVIKSPGIS PYSPLAVAAT AAGAHFIGGT QLWFAAHADT DGVVPGAVCV
TGTKGKSTTT ALLAHLLRAA GHCTALAGNI GMPLLELLTP QPTPEYWAIE LSSYQTGDVA
RSGARPVLAL VLNVFPEHLD WHGSEQRYIN DKLSLVTVTR PRIALLNAAD PRLASLALPQ
SDLRWFNRRD GWHVRGQVVY RGDRAVLDTA LIPLPGAHNG SNVCAVLATL EALGLNAVAL
APAACNFHPL PNRLQFLGER DGILWVNDSI STTPHATLAA LDCFLGRCRV AVLVGGYDRG
VDWECFAARI TRKVPLDIVT MGANGPHIQA LLAPLAAGRF GLHAAVDLPQ AVALARTALG
AQGGVLLLSP GAPSFGAYQD YVARGRHFAI LAGFDPEVIS SISGLGIA
