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Database: UniProt
Entry: A0A0G0LQD7_9BACT
LinkDB: A0A0G0LQD7_9BACT
Original site: A0A0G0LQD7_9BACT 
ID   A0A0G0LQD7_9BACT        Unreviewed;       666 AA.
AC   A0A0G0LQD7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=UDP-N-acetylmuramate-L-alanine ligase {ECO:0000313|EMBL:KKQ90180.1};
GN   ORFNames=UT12_C0001G0048 {ECO:0000313|EMBL:KKQ90180.1};
OS   Candidatus Curtissbacteria bacterium GW2011_GWC2_38_9.
OC   Bacteria; Candidatus Curtissbacteria.
OX   NCBI_TaxID=1618414 {ECO:0000313|EMBL:KKQ90180.1, ECO:0000313|Proteomes:UP000034893};
RN   [1] {ECO:0000313|EMBL:KKQ90180.1, ECO:0000313|Proteomes:UP000034893}
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:KKQ90180.1}.
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DR   EMBL; LBVP01000001; KKQ90180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0LQD7; -.
DR   PATRIC; fig|1618414.3.peg.48; -.
DR   Proteomes; UP000034893; Unassembled WGS sequence.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like 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   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKQ90180.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT   DOMAIN          10..245
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          248..342
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          353..480
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          526..609
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   666 AA;  74933 MW;  09B0ED40E6B05ED1 CRC64;
     MQNKKLPFAV IVLAAGEGKR MESKLSKVLH RIAGKPMIVR TIEILKRVNP YEIIIVANPQ
     NLVAIKKEIP QDVKYTIQKS PLGTADAASC GLKLVDKNML TVAVMYGDDS AFYRPETILE
     VFKHHQDSDA TLTFVTVKKD DPTDFGRIVR KDGKVVSIVE EKDTSAVQKK INEVNASLYF
     FDKRWLLQNL TKIKPSPVTS ELYITDLIAI ATGDNQKVET FPLGDENEWQ SVNTKEELLA
     VNLNFQKRIH IMGIAGAGAA AIAGIAKATG FEVTGCDLNP KSPYTQNLKI KIRSGHNPSH
     IEDIGMLVIS PAVLKFNPKN QELKYAKEVQ IPILTWQEFQ GKYLQKDKFV ICVAGAYGKS
     TTTTMIAKTL TDLGKDPTCE IGATVLEWQQ NFRVGKSNYY VCEADEYNDN FLNYQPDIAV
     VLNLDWDHPD YFKTKKQLFG SYKKFVSKIK KNGTLIIPNT WNFTQLTKFI RKDIKVIKIG
     DFGKLDLSII GDFRSENANA ALTVAKVLGL NITKAKKSIE NFKGIARRLE YKGEVNDVKV
     YDDYAVQPYT VLKTANALEE KFKDKKVVLV FEPHTFSRIK TFFNDFVKNL KKSRVDKILV
     TEVYAAREKG DRSKLAQKLA QSVGPKATFT GSLKETAMYL KNHLADFDII LLMGAGDVYK
     LYEMLL
//
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