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Database: UniProt
Entry: A0A1Z4FW08_9CYAN
LinkDB: A0A1Z4FW08_9CYAN
Original site: A0A1Z4FW08_9CYAN 
ID   A0A1Z4FW08_9CYAN        Unreviewed;       500 AA.
AC   A0A1Z4FW08;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=NIES2098_25970 {ECO:0000313|EMBL:BAY09435.1};
OS   Calothrix sp. NIES-2098.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1954171 {ECO:0000313|EMBL:BAY09435.1, ECO:0000313|Proteomes:UP000218444};
RN   [1] {ECO:0000313|EMBL:BAY09435.1, ECO:0000313|Proteomes:UP000218444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2098 {ECO:0000313|EMBL:BAY09435.1,
RC   ECO:0000313|Proteomes:UP000218444};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; AP018172; BAY09435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4FW08; -.
DR   KEGG; caln:NIES2098_25970; -.
DR   OrthoDB; 9800958at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000218444; Chromosome.
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};
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          27..104
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          116..317
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          338..425
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   MOTIF           415..418
FT                   /note="Meso-diaminopimelate recognition motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         34
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         118..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         160..161
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         187
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         193
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         195
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         391
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   BINDING         415..418
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   BINDING         470
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT   MOD_RES         227
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
SQ   SEQUENCE   500 AA;  53691 MW;  33EDAA3096CE3B4B CRC64;
     MKLRELLAAI DSVEQLPKHP ALADAEVQGL KTNSHACGVG DLFIGMPGTR VDGGEFWQSA
     IASGAVAAVV SPQAVQKNPP TSEAVVISAS DMTKACAQLA GAFYGYPGRK LKLVGVTGTN
     GKTTTTHLIE FLLGKANQPT ALMGTLYTRW PGFAETAVHT TPFAVELQQQ LAQAVDAGCE
     YGVMEVSSHA LAQGRVLGCE FEVAVFSNLT QDHLDFHRDM EDYFAAKALL FSPDYLKGRA
     IINADDPYGK RLIGALSPEK VWSYSVNNAN ADFWMSDLNY EPNGVSGTLH TPKGNVAFRS
     PLVGQYNLEN LLAAVGAVLH LGLDLQLVAA AISEFPGVPG RMERVQVIPN QDISVIVDYA
     HTPDSLENLL KAARPFIPGK MICVFGCGGD RDRTKRPKMG KIAAELADVA VVTSDNPRTE
     DPQKILQDIL AGIPETIHPT VIGDRAAAIR TAILQAQPGD GVLLAGKGHE DYQILGTEKI
     HFDDREHARA ALQERLKIQN
//
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