ID A0A364K726_9BACL Unreviewed; 495 AA.
AC A0A364K726;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
DE EC=6.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00208};
DE AltName: Full=Meso-A2pm-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
DE AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
DE AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
GN Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
GN ORFNames=DL897_08090 {ECO:0000313|EMBL:RAL26012.1};
OS Thermoflavimicrobium daqui.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoflavimicrobium.
OX NCBI_TaxID=2137476 {ECO:0000313|EMBL:RAL26012.1, ECO:0000313|Proteomes:UP000251213};
RN [1] {ECO:0000313|EMBL:RAL26012.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL26012.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Wang X., Zhou H.;
RT "Thermoflavimicrobium daqus sp. nov., a thermophilic microbe isolated from
RT Moutai-flavour Daqu.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAL26012.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL26012.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Zhirakovskaya E.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the
CC nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG)
CC in the biosynthesis of bacterial cell-wall peptidoglycan.
CC {ECO:0000256|HAMAP-Rule:MF_00208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-
CC muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-
CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-
CC diaminoheptanedioate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791,
CC ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216;
CC EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00208,
CC ECO:0000256|RuleBase:RU004135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
CC ECO:0000256|RuleBase:RU004135}.
CC -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC consequently, for the gamma-phosphate positioning of ATP.
CC {ECO:0000256|HAMAP-Rule:MF_00208}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC {ECO:0000256|ARBA:ARBA00005898, ECO:0000256|HAMAP-Rule:MF_00208}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
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:RAL26012.1}.
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DR EMBL; QJKK01000003; RAL26012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364K726; -.
DR OrthoDB; 9800958at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000251213; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate 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; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR HAMAP; MF_00208; MurE; 1.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
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; IPR035911; MurE/MurF_N.
DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR NCBIfam; TIGR01085; murE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR Pfam; PF01225; Mur_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.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00208};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00208};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00208};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00208};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:RAL26012.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00208}; Reference proteome {ECO:0000313|Proteomes:UP000251213}.
FT DOMAIN 22..94
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 106..314
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 334..420
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT MOTIF 409..412
FT /note="Meso-diaminopimelate recognition motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 30
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 108..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 149
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 150..151
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 177
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 185
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 385
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 409..412
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 462
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 466
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT MOD_RES 217
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
SQ SEQUENCE 495 AA; 54900 MW; 5D1BA264040125AC CRC64;
MRLEDIIQPL ILKQVIGDLG TEIKGIKIDS RQVESGDLFI ALRGLTVDGH RFIDKAISQG
AAAVMVEEPI SANIPVVIVP DTRRAMAMAA ATFYRHPTKE LKVIGVTGTN GKTTTTNLIQ
HILNDQDQKT GLIGTISMKV GNREYKVNNT TPEIVDLQRS FRWMLDEGCK YAAIEVSSHG
LVMGRTRGCE FHIAVFTNLT QDHLDYHETM EKYRDAKGLL FNQLGTRYSD DPQFNQVAVL
NADDPVSKHY ANTTSAQVIT YGIDQKADVR AENIRITATG TRFMLRSFGG DIEMNLQLVG
KFNIYNALAA VSVALLEGIS LEKVKKSLES ISGVNGRFER VQAGQNFTVL VDYSHTPDSL
ENALQTIREF VDGRVICVVG CGGDRDRSKR PVMAQIAEKY SDLTIITSDN PRTEPPEEII
AEMVAGIKGV NLKRYETIVD RREAIHFAIH QAKANDVVLI AGKGHETYQE INGVRYDFDD
RLVAKAAIES RRSEG
//
