ID   A0A0G0L6C3_9BACT        Unreviewed;       438 AA.
AC   A0A0G0L6C3;
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:KKQ86572.1};
GN   ORFNames=UT09_C0031G0009 {ECO:0000313|EMBL:KKQ86572.1};
OS   Parcubacteria group bacterium GW2011_GWF2_38_8.
OC   Bacteria.
OX   NCBI_TaxID=1618961 {ECO:0000313|EMBL:KKQ86572.1, ECO:0000313|Proteomes:UP000034262};
RN   [1] {ECO:0000313|EMBL:KKQ86572.1, ECO:0000313|Proteomes:UP000034262}
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:KKQ86572.1}.
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DR   EMBL; LBVM01000031; KKQ86572.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0L6C3; -.
DR   PATRIC; fig|1618961.3.peg.596; -.
DR   Proteomes; UP000034262; 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; 2.
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:KKQ86572.1}.
FT   DOMAIN          31..83
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          102..248
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          271..349
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   438 AA;  48874 MW;  742E164677EA610A CRC64;
     MRTIFKKIVA YILQAESRLV VWKYKPKIVA ITGSIGKTST KDTIYAVLSG ISYVRKSEKS
     YNSEIGLPLT ILGCPNGWNN FFVWLLNIFK GLWLFVWPHK YPDWLVLEAG VGKPNDMRHT
     ASWLKTDAVV ITAIGETPAH IEFFDSHKHL VEEKSGLIKT LKKDGLLVLN NDDEIVSEMR
     AKTKNRVITF GFRKSSDIIC SDDSISYNDA GIPHGIIFRI EERGSSLPVA IEGAFGKNHV
     YASLGALALS SGLKFNMLKA IEALKNYNAP PGRMRLLRGM NNSLIIDDTY NSSPFACQSA
     LKTLGEVRSV GRKIAVLGDM LELGRHTEES HKNVGKVAKE NADVLFIVGP RAKFIKEGAM
     EVYPAMGGTG MTADNIFEFS NSCEAGEYLK TFVRENDFVL LKGSQGMRME RAVEAILLDQ
     ENKSNLLVRQ DEEWLKKK
//