ID   A0A0G0QZ79_9BACT        Unreviewed;       399 AA.
AC   A0A0G0QZ79;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase {ECO:0000313|EMBL:KKR42731.1};
GN   ORFNames=UT77_C0001G0182 {ECO:0000313|EMBL:KKR42731.1};
OS   Candidatus Daviesbacteria bacterium GW2011_GWC2_40_12.
OC   Bacteria; Candidatus Daviesbacteria.
OX   NCBI_TaxID=1618431 {ECO:0000313|EMBL:KKR42731.1, ECO:0000313|Proteomes:UP000034881};
RN   [1] {ECO:0000313|EMBL:KKR42731.1, ECO:0000313|Proteomes:UP000034881}
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   -!- 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:KKR42731.1}.
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DR   EMBL; LBYB01000001; KKR42731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0QZ79; -.
DR   PATRIC; fig|1618431.3.peg.184; -.
DR   Proteomes; UP000034881; Unassembled WGS sequence.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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   PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE 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.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:KKR42731.1}.
FT   DOMAIN          49..235
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          257..334
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   399 AA;  44272 MW;  2B89ACC8F31A1E9D CRC64;
     MDIAKHPIWN QVTPYKTKIP SFKKPFHLLR IYLARQYAKL YPQDMFVGVT GSVGKTACVA
     ACAAVCSQKY KTLATKQDLD PVLNIPATLL KLNPSTKKVI LEMGVEYKGE MDFYLSQVRP
     KTVVVTRISY AHSETLGDID GILQEKGKLV ESLDENGLAI LNWDDLSSRR LAASCRGTVM
     YYGMDPKNCT VWAGNPKIEN FTTNFELNLG VERVKVNFKL LGLHQVYPAL AAALLGVSLG
     IPLTKIKKAL ESVEPLEHRM QALAGPNGSI LLDDTYNSSP AAMDAAIDTL LAVPSRRKVI
     VLGEMRELGP YSEKLHRQVA QRIYQEKLDL VFLGQGEAQI IGDELKSLGF WQERLESNLT
     NSQIVSKLLK NLGKGDVCLI KGSRVVRLDE VVKRIAKKS
//