ID   A0A0G1RX27_9BACT        Unreviewed;       453 AA.
AC   A0A0G1RX27;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   SubName: Full=UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase {ECO:0000313|EMBL:KKU61646.1};
GN   ORFNames=UX85_C0002G0026 {ECO:0000313|EMBL:KKU61646.1};
OS   Candidatus Beckwithbacteria bacterium GW2011_GWB1_47_15.
OC   Bacteria; Candidatus Beckwithbacteria.
OX   NCBI_TaxID=1618371 {ECO:0000313|EMBL:KKU61646.1, ECO:0000313|Proteomes:UP000033860};
RN   [1] {ECO:0000313|EMBL:KKU61646.1, ECO:0000313|Proteomes:UP000033860}
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:KKU61646.1}.
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DR   EMBL; LCNT01000002; KKU61646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1RX27; -.
DR   PATRIC; fig|1618371.3.peg.315; -.
DR   Proteomes; UP000033860; 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:KKU61646.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          137..278
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   453 AA;  50592 MW;  6BA231120D436CB4 CRC64;
     MIDFFKLIYF ILVFKAILRC VYFWQLKEYR LDRFREFLTT SESGAYFLPT NRLLRPKFTL
     KVWLLIYLAF YFTLYLLNAF PQNRLWAAML AYLLLPVSVA VSVALLAPAT SLVYDLAIFL
     AKIKIHLTGS RLTVVGITGS YGKTATKEIL AHLLAGRYRV LKTPANVNTA VGVAKTVLTR
     LSPSHQVFVV EMGAYRRGEI QKICRLVTPQ IGVLTGINQQ HLGLFGSFSN LLATKYELIA
     SLPKNGLAVV NGANKFCRDL AKKTNHVPVR LYSKPKKAFK TNLLGSWQQL NIAAAVTVAR
     RFKVKPAAIK KLLFSIPSFK TALKVRRGEK GLTILDDSYN SNPAGFLAAV NFAKAKKARA
     KILVTAGIIE TGSAKKDIHE KLAHKSLSVF KQVTVTKKDT YRLFLAAAKK DQTKKLSFAP
     DFNQIIVSLK NQANPQSLVL FEGRFPEKLI ASL
//