ID   A0A0G1GE56_9BACT        Unreviewed;       388 AA.
AC   A0A0G1GE56;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase {ECO:0000313|EMBL:KKS97148.1};
GN   ORFNames=UV74_C0013G0270 {ECO:0000313|EMBL:KKS97148.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWB1_43_14.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618578 {ECO:0000313|EMBL:KKS97148.1, ECO:0000313|Proteomes:UP000034090};
RN   [1] {ECO:0000313|EMBL:KKS97148.1, ECO:0000313|Proteomes:UP000034090}
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:KKS97148.1}.
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DR   EMBL; LCFQ01000013; KKS97148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1GE56; -.
DR   STRING; 1618578.UV74_C0013G0270; -.
DR   Proteomes; UP000034090; 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; 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; 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:KKS97148.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        53..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          113..236
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   388 AA;  44866 MW;  0555A5E12D55D11F CRC64;
     MSKILSTIYP IADFLYLLQL EEYESKRYFN TIKRFWWRRN IQKRGKLVYT KRINITLALA
     LPFCITMPPF TPLWIWLSNS VLTPYFERIK LNIQKNAAIH FNKYGKNTKV IAIAGSYGKT
     TVKNYIYEFV RYNYKTQIIP GNINTPTGIA NWLLNNFDHS SELLIVEVDT YFVGEIKRSL
     RITPPDIALL TNVGDQHLER LGSKSNLKKA LLEIFDYAKP NAIKICDKKT NLAYALKVAK
     ILNIPNDIIK DTITKLKKPD RRGDVKIINK FKVIDQSYNI SGDTAKYGVD NAVKLAKLDK
     KGLIVITAGI PELGEENKYA NKKLGKYLVK KVHKIILLKS ILYTEVINNS NKFILANNLN
     DAWKILEEYD PKKYLILLQP ELNDLYYE
//