ID A0A0G0XEZ6_9BACT Unreviewed; 341 AA.
AC A0A0G0XEZ6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-2, 6-diaminopimelate ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=UU83_C0051G0008 {ECO:0000313|EMBL:KKS23410.1};
OS Candidatus Jorgensenbacteria bacterium GW2011_GWF2_41_8.
OC Bacteria; Candidatus Jorgensenbacteria.
OX NCBI_TaxID=1618667 {ECO:0000313|EMBL:KKS23410.1, ECO:0000313|Proteomes:UP000033856};
RN [1] {ECO:0000313|EMBL:KKS23410.1, ECO:0000313|Proteomes:UP000033856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS23410.1}.
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DR EMBL; LCCD01000051; KKS23410.1; -; Genomic_DNA.
DR PATRIC; fig|1618667.3.peg.688; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000033856; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..248
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 270..317
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 341 AA; 38396 MW; B3BDB4F2B94E663C CRC64;
MFKEGLLDKI LYQVKKLIPK SVFIFFVPFY HAGLAYAGAV LYGFPSRKMK VIGVTGTKGK
STTVFLISKI LESADKKIAA IGSLGFKIRE REWPNTLKMT MPGRFKLQKF LYEAKKAGCE
FVVLEVTSEG IKQKRHLGIS FDCAVFTNLH KEHIESHGSF ENYRKAKEEL FSATKNIHVL
NADDPNVEYF SRYPVKRKMF FGLQTGDMKA NNIENTEKGI KFDVYGTVFN LNLAGEFNVQ
NCLAALAVSA MYGIDLPSAK PILEEIKSIS GRMEFIQKEP FRVVVDYAHT PDSLESVYKT
LKTQNPKNPK LICVLGXXXX XXXXXGKGRN SAESRKNIAM K
//