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Database: UniProt
Entry: A0A1Y2LFW3_9PROT
LinkDB: A0A1Y2LFW3_9PROT
Original site: A0A1Y2LFW3_9PROT 
ID   A0A1Y2LFW3_9PROT        Unreviewed;       486 AA.
AC   A0A1Y2LFW3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-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=TALK_04070 {ECO:0000313|EMBL:OSQ49527.1};
OS   Thalassospira alkalitolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassospiraceae; Thalassospira.
OX   NCBI_TaxID=1293890 {ECO:0000313|EMBL:OSQ49527.1, ECO:0000313|Proteomes:UP000193396};
RN   [1] {ECO:0000313|EMBL:OSQ49527.1, ECO:0000313|Proteomes:UP000193396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18968 {ECO:0000313|EMBL:OSQ49527.1,
RC   ECO:0000313|Proteomes:UP000193396};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Thalassospira alkalitolerans JCM 18968.";
RL   Submitted (MAR-2014) 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:OSQ49527.1}.
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DR   EMBL; JFKB01000002; OSQ49527.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2LFW3; -.
DR   STRING; 1293890.TALK_04070; -.
DR   OrthoDB; 9800958at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000193396; 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:OSQ49527.1};
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}.
FT   DOMAIN          24..99
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          109..311
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          332..416
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   MOTIF           408..411
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         384
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         408..411
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   BINDING         460
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;  51375 MW;  A69EB4CD66E4ADFE CRC64;
     MRLSELMAGD QAALKHADGQ DPNITGLTAD SRTVKDGYLF AALSGAKTDG SKYIEDAIRL
     GAAAILAKDG TPKPIAATVP LIPVENPRLR YAQLAARFYG QQPANIAAIT GTNGKTSTAV
     FTEQLWTLLG NTSGSIGTLG IRAAGTKIPG ALTTPDPVAL HQSLNEMVEI GVTHVAMEAS
     SHGLDQYRLD GVKVSVAAFT NLTRDHLDYH GNFEKYFAAK ARLFSDLLVE NGTAVLNADV
     PQFKVLRSMC QGRGVTVMSY GHDADDIKLI DAKPTATGTK LKLAIDKGEY GVHLPLMGEF
     QVMNALAALG IVIASGADID DAVAALEKLE GVRGRMELVG STSFGSPVFV DYAHTPDALE
     TVIKAVRPHC KGRIICVFGA GGDRDTGKRP EMGRIVHQNA DIAIITDDNP RSEDPATIRA
     AIKKACDGAV EIGDRAEAIK RGIGILQRND ILIIAGKGHE RGQIIGDTVL PFDDAAIARN
     ILLGGN
//
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