ID A0A0G1X8Q7_9BACT Unreviewed; 420 AA.
AC A0A0G1X8Q7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE SubName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000313|EMBL:KKU90730.1};
GN ORFNames=UY22_C0050G0005 {ECO:0000313|EMBL:KKU90730.1};
OS Candidatus Amesbacteria bacterium GW2011_GWC1_48_10.
OC Bacteria; Candidatus Amesbacteria.
OX NCBI_TaxID=1618365 {ECO:0000313|EMBL:KKU90730.1, ECO:0000313|Proteomes:UP000034877};
RN [1] {ECO:0000313|EMBL:KKU90730.1, ECO:0000313|Proteomes:UP000034877}
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:KKU90730.1}.
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DR EMBL; LCPE01000050; KKU90730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1X8Q7; -.
DR PATRIC; fig|1618365.3.peg.975; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000034877; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; 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; 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.
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 36..195
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 237..324
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 420 AA; 46811 MW; AAFE4C60448785EF CRC64;
MKWWGQRVKN IYHYLVSVAM IIWCRYPAKK LFVIGVTGTD GKTTTATLIY EILRAAGLNA
ALISTVAAKI GGEEVDTGLH TTNPDARRMQ PLLRRMADAG VTHLVLEVTA HGLDQYRVLG
CNFAVGVLTN ITHEHLDDFV TMERYRRAKL KLFKGVKFAV LNADDPSFKN FQFSIFNFKS
NSKTRIIKYS KSKLKNISPA LWGDYNRYNI GAAEAVARIL EVRSQIVETV IKDFEGVPGR
REEVKAGQKF RVIVDFAHTP NALDQVLLQL RKELGAEKRL ILVFGCTGER DKGKRPMMGE
IASRLADVVI ITSDDMRSES QDEIARQIMS GITPELRSSP LKFSSPTRVF AVRGDKRGDM
KIVKENDRGE AIKKAIKEAG PGDIVLLAGK GHERTILIGK TERPWSDAEE AKRAIRGAGG
//
