ID A0A1B6YCA1_9BACT Unreviewed; 486 AA.
AC A0A1B6YCA1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=A8B79_15315 {ECO:0000313|EMBL:OAN63441.1};
OS Balneola sp. EhC07.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN63441.1, ECO:0000313|Proteomes:UP000078514};
RN [1] {ECO:0000313|EMBL:OAN63441.1, ECO:0000313|Proteomes:UP000078514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC08 {ECO:0000313|EMBL:OAN63441.1,
RC ECO:0000313|Proteomes:UP000078514};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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|HAMAP-Rule:MF_00208, 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:OAN63441.1}.
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DR EMBL; LXYG01000008; OAN63441.1; -; Genomic_DNA.
DR RefSeq; WP_066218116.1; NZ_LXYG01000008.1.
DR AlphaFoldDB; A0A1B6YCA1; -.
DR STRING; 1849360.A8B79_15315; -.
DR InParanoid; A0A1B6YCA1; -.
DR OrthoDB; 9800958at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000078514; 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: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; 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.
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:OAN63441.1};
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:UP000078514}.
FT DOMAIN 30..93
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 109..300
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 322..412
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT MOTIF 401..404
FT /note="Meso-diaminopimelate recognition motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 31
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 111..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 153..154
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 180
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 186
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 188
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 377
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 401..404
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 452
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 456
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT MOD_RES 220
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
SQ SEQUENCE 486 AA; 52742 MW; 9836AE9C4E34FBF6 CRC64;
MNTHDLIEFI NPLNTSRFKP EGEVGPLVQD SRQVTESSVF IAIRGTEVDG HMFLEDAIHR
GAKVIICEES YYTDAEVCVI EVENTRSLIG PLAQKMAGNP GDKLKIIGIT GTNGKTTTAT
LVYQALTKLG EKVSLLGTVE KKILTEALDS KLTTADPIEL AADMKKMVEA GSEYLVMEVS
SHALHQARVG GFDFKVAAFT NLSQDHLDYH ETIEEYAAAK KILFDGLKPG SSAVINMDDS
YGVFMADGIS AQISELSFGK NAHVLSNSAQ GLKISVDGSE ISSSLVGHFN AFNLAEAFMI
CNELGHDKQR IASALSSVPG APGRMESVNL DLETDLPKVI VDYAHTPDAL ENVLKTLSES
RTQNQFIYCV FGAGGDRDSG KRPEMAKAAL EFADEIIVTS DNPRTENPDL IIADILQGFE
NTDNVVTITS RKEAIFKAIE LASSNDIILI AGKGHEDYQE IDGKRYPFDD RLVAKEALEL
KAKGGF
//
