MURD2_MICS3
ID MURD2_MICS3 Reviewed; 452 AA.
AC C4RJF7;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305};
DE EC=6.3.2.53 {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000269|PubMed:28294606};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-L-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305};
DE Short=UDP-MurNAc-L-Ala-L-Glu synthetase {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000303|PubMed:28294606};
GN Name=murD2 {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000303|PubMed:28294606};
GN ORFNames=MCAG_01009 {ECO:0000312|EMBL:EEP70682.1};
OS Micromonospora sp. (strain ATCC 39149 / NRRL 15099 / SCC 1413).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora; unclassified Micromonospora.
OX NCBI_TaxID=219305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39149 / NRRL 15099 / SCC 1413;
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Galagan J., Nusbaum C., Birren B.;
RT "The genome sequence of Micromonospora carbonacea var. africana strain ATCC
RT 39149.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 39149 / NRRL 15099 / SCC 1413;
RX PubMed=28294606; DOI=10.1021/jacs.7b01221;
RA Feng R., Satoh Y., Ogasawara Y., Yoshimura T., Dairi T.;
RT "A glycopeptidyl-glutamate epimerase for bacterial peptidoglycan
RT biosynthesis.";
RL J. Am. Chem. Soc. 139:4243-4245(2017).
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, ECO:0000269|PubMed:28294606}.
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 ECO:0000269|PubMed:28294606};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305|PubMed:28294606}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02208,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurD2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305}.
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DR EMBL; GG657738; EEP70682.1; -; Genomic_DNA.
DR RefSeq; WP_007071958.1; NZ_GG657738.1.
DR AlphaFoldDB; C4RJF7; -.
DR SMR; C4RJF7; -.
DR STRING; 219305.MCAG_01009; -.
DR EnsemblBacteria; EEP70682; EEP70682; MCAG_01009.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_032540_4_1_11; -.
DR OMA; CNFENYL; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000010307; 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: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 1: Evidence at protein level;
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..452
FT /note="UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase"
FT /id="PRO_0000446508"
FT BINDING 118..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02208"
SQ SEQUENCE 452 AA; 47604 MW; 04CCCDEC5450E870 CRC64;
MRLSDLRGRT VAVWGAGREG RAAVIAIAAH GPADLVAVDD SANFLALPWE GPLAEAAPLV
TGEEGFARLA AAEVVVRSPG VPNTHPWLVE LRGRGVTVTQ GSALWMADHA RRTVGVTGSK
GKSTTSSLIS HLLTAVDRPN VFGGNIGVPL LDLPDADLYV LELSSYQCAD LTDSPRVAVV
TALFPEHLDA HGGEREYYRD KLNLLAHGPQ TIVVNGADPR LAAELGDRPA VRAGSPDTTH
VAPGPDGTPW FHLGDRPLFP RAVLPLVGRH NEGNLCVALA VLAALGVDVV ARADALAVAV
AGFQGLAHRL TEIADPSGLT FVDDTLATSP YAAMHAIDAY EGRPVTVIVG GADRGLDYAP
LREHLAEREI TVLGIPDSGQ RIVATLAGLP RVRAEVVDDL VAAVRRAREL TPADGVVLLS
PAAPSYGRFR NFEHRSEVFA EAVRDTAGHP AR
