ID   A0A0G0B664_9BACT        Unreviewed;       407 AA.
AC   A0A0G0B664;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   SubName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000313|EMBL:KKP59196.1};
GN   ORFNames=UR52_C0010G0009 {ECO:0000313|EMBL:KKP59196.1};
OS   Candidatus Gottesmanbacteria bacterium GW2011_GWA1_34_13.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1618434 {ECO:0000313|EMBL:KKP59196.1, ECO:0000313|Proteomes:UP000034176};
RN   [1] {ECO:0000313|EMBL:KKP59196.1, ECO:0000313|Proteomes:UP000034176}
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:KKP59196.1}.
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DR   EMBL; LBPN01000010; KKP59196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0B664; -.
DR   STRING; 1618434.UR52_C0010G0009; -.
DR   Proteomes; UP000034176; 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; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 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;
FT   DOMAIN          33..212
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          233..314
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   407 AA;  45734 MW;  58A318AF0689DC29 CRC64;
     MWQSIKNKFH GLNACLAALF YGFPGKKIKI IGVTGTDGKT TTTHLIHWIL TQSGKKTSMI
     SSVYASIAGN IFDTGFHVTT PNPWVLQKLI NIAVKNGDEF LILEVTSHSI DQKRISGNNF
     LVGVVTNVTP EHLDYHKNYE DYLHIKSQLL EHAKYAVLNK DDGSYKYLNT INKNITTYAV
     RNNADVTPQN FPFSTSLPGE YNIANNLAAI SVCKILKIKD NIIRNAVKEF KGVKGRFELI
     KNNKGIRIIV DFAHTPNAFK QILPLVKSQT QGKLIHIFGC AGLRDESKRP VMGRISAQNA
     DIIILSEEDY RTENVNTIID NIAQGCKQAH GIELKINQLE KLDDIETPVF FRISDRQTAI
     DFVFNKVVRE GDTVILTGKA HEQSLCRGNK EYSWDEFKAV EKALLIN
//