ID   A0A0G1WER6_9BACT        Unreviewed;       484 AA.
AC   A0A0G1WER6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   SubName: Full=UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase {ECO:0000313|EMBL:KKW17273.1};
GN   ORFNames=UY57_C0020G0012 {ECO:0000313|EMBL:KKW17273.1};
OS   Candidatus Kaiserbacteria bacterium GW2011_GWB1_50_17.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1618673 {ECO:0000313|EMBL:KKW17273.1, ECO:0000313|Proteomes:UP000034120};
RN   [1] {ECO:0000313|EMBL:KKW17273.1, ECO:0000313|Proteomes:UP000034120}
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:KKW17273.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LCQM01000020; KKW17273.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1WER6; -.
DR   Proteomes; UP000034120; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:KKW17273.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        65..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          150..329
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          354..429
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   484 AA;  54075 MW;  4D0E23D9C1DFDA1C CRC64;
     MNNKRQTVNG AKRWLSRRHW NYIRSLVYML QASEYIIVDF LKWHERVKDF RFVEKRKHLT
     FTPKTVILFT LGWIVLLATL SGAVFVFYTI ASPWNYLLAA LLVFEAPLIA MVSLLFFVIC
     MRFAQYPVEQ FFIARTKKHL IAHRGIKIAI AGSFGKTSMR EVLKAVLSEG RKVAAPGESY
     NTPLSIARFV KELKGDEDVL IFELGEYYPG DVRKLAQMVR PEWGIITGVN EAHLEKFGVL
     KNTTDTVFEL AESVDASRLY VNGESELARA RSKGGNILYT RSGTEEWQVK NPNTDLSGIT
     FTLLKNGVSI NVHSSVCGLH VLGPLSAAVH IASRLGLASH EISDGIAKTK PFAHRLEPKQ
     WPDGVTFIDD SYNGNPDGAR AAIEFLASLQ GRRFYVTPGL VEAGLRIKEV HEEIGKQLAK
     AGIEKVVLIR TSVASYMESG LQAGDFKGEI LRYDDMPSAL AALRALALPG DVILIQNDWP
     DQYA
//