ID A0A1G2EXL0_9BACT Unreviewed; 413 AA.
AC A0A1G2EXL0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2931_04545 {ECO:0000313|EMBL:OGZ30252.1};
OS Candidatus Niyogibacteria bacterium RIFCSPLOWO2_01_FULL_45_48.
OC Bacteria; Candidatus Niyogibacteria.
OX NCBI_TaxID=1801724 {ECO:0000313|EMBL:OGZ30252.1, ECO:0000313|Proteomes:UP000177486};
RN [1] {ECO:0000313|EMBL:OGZ30252.1, ECO:0000313|Proteomes:UP000177486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|RuleBase:RU004135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004135}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC {ECO:0000256|ARBA:ARBA00005898}.
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:OGZ30252.1}.
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DR EMBL; MHMQ01000024; OGZ30252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2EXL0; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000177486; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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-UniPathway.
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 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; 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; 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 PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU004135};
KW Cell division {ECO:0000256|RuleBase:RU004135};
KW Cell shape {ECO:0000256|RuleBase:RU004135};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004135};
KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135}.
FT DOMAIN 44..202
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 247..331
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 413 AA; 46034 MW; D61111312A2B2E83 CRC64;
MNFTKKFIPG PVLDFLRPIY HRLFSVLSVV FYGRPSREMV VVGITGTNGK TSVVEYITQI
LREAGIKTAS VSSLYFRIGD EAEKNTLKMT MPGRFFLQKF LRRALKAGCT HAVLEITSEG
IRQFRHKNID WDVLVLTNIT PEHIESHGSF ENYRKAKEKV FAELSKTYCK SDVAKTFIIN
GDDPAAPEFL KYEADKKIIY SKKDAPRELK LLGEFNLYNI AAAVKTAQAL GIPQEVITKA
VEKIEGVPGR MEFVQREPFV VVVDYAHTPD ALRKVYETLR PPASGRLICV LGSAGGGRDK
WKRPEMGKIA SEFCQEIILT NEDPYDEKPE VIIEDIFGGI AGIRSPGILG SNPGVLEIID
RKEAIKKAIS DAKTGDVVVI TGKGAEPWIM GPGGTKTPWD DREIAREALK NKE
//