ID A0A133XUT4_9ACTN Unreviewed; 582 AA.
AC A0A133XUT4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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};
GN Name=murD {ECO:0000256|HAMAP-Rule:MF_00639};
GN ORFNames=HMPREF3192_00758 {ECO:0000313|EMBL:KXB34659.1};
OS Atopobium deltae.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Atopobium.
OX NCBI_TaxID=1393034 {ECO:0000313|EMBL:KXB34659.1, ECO:0000313|Proteomes:UP000070675};
RN [1] {ECO:0000313|Proteomes:UP000070675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00019 {ECO:0000313|Proteomes:UP000070675};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- 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:KXB34659.1}.
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DR EMBL; LSCR01000012; KXB34659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133XUT4; -.
DR STRING; 1393034.HMPREF3192_00758; -.
DR PATRIC; fig|1393034.3.peg.732; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000070675; 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: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; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00639; MurD; 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 NCBIfam; TIGR01087; murD; 1.
DR PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000070675}.
FT DOMAIN 184..366
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT REGION 79..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ SEQUENCE 582 AA; 62892 MW; B01DFF48B48E6A4B CRC64;
MGMTRQNVNE QRADEKTVGA ASVGEKCISA AVADEKTVDE KTLGDVCILG VGKTGVAVAQ
YLLDLPRGTV RSITMYGGTQ SGAHAREPQT HEAQVHEAHT HESQQQQQPA DDPLQNLADA
GVRLVLGTDE VKAPANVAAY NLTITSPGIP PFSRFYQTAA SCSKTMIGEP EFAWRQSPDK
WIGITGTNGK TTTTTLIAAL LQQAGLLAKA VGNIGTLSIA NVAKRPADEW FVAELSSFQL
AETQHLHPRV AILLNITPDH LSWHKTLQNY VAAKERIFAQ LDAGDLAVIS SDSNLTPIVE
RLHKRGLRVC ICDTAADPHT PCAAFVAEKT LYVRLDAKLY ALLGVDELTL KGTHNIQNVL
AACACALDLG LSVESICQTL RSFSPLEHRI EPVATDAAGI HYINDSKATN TDAVVKALTA
FPKGKVILLA GGHDKHTELT EFNQAVLESC KAVVCFGEAA SRLSEALSTY QEQTQVSGQN
QTSQQDQRQT DDPRLRIEHA KHLADALQQA IALAHKGDYV LLSPACSSFD EFSGYEERGR
VFKQLVMQHV NQHLNHAANS DSETTSPDKT TDNNPKECEK SS
//
