ID A0A0G1N4C8_9BACT Unreviewed; 324 AA.
AC A0A0G1N4C8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=UDP-N-acetylmuramate-L-alanine ligase {ECO:0000313|EMBL:KKU15461.1};
GN ORFNames=UX23_C0001G0060 {ECO:0000313|EMBL:KKU15461.1};
OS Parcubacteria group bacterium GW2011_GWB1_45_9.
OC Bacteria.
OX NCBI_TaxID=1618879 {ECO:0000313|EMBL:KKU15461.1, ECO:0000313|Proteomes:UP000034512};
RN [1] {ECO:0000313|EMBL:KKU15461.1, ECO:0000313|Proteomes:UP000034512}
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:KKU15461.1}.
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DR EMBL; LCLK01000001; KKU15461.1; -; Genomic_DNA.
DR PATRIC; fig|1618879.3.peg.66; -.
DR Proteomes; UP000034512; 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; 2.
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 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 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.
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:KKU15461.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 6..89
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 94..258
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 286..318
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 324 AA; 36186 MW; CC2189C21E5BC402 CRC64;
MNKKIVHFIG IGGIGVSALA GWFKAYGWEV SGSDIETTGH SPSLLPKDAR LVIYSNAISP
DNPELKKAKK LGIKTFSYPE ALGELTKAHR TIAVAGSHGK STTTALLSLI LIKAGFDPTV
IIGTKLREFG DSNFKYGKSN YLVIEADEWK GAFWHYSPTF AVITNIDKEH LDFYKNFNNV
KKSFLKFIGN IHSSGVLVVN KDDKPLYALR GSIKKIAKKN KFKVLWYGKN QKTVPKIKKV
LQLPGAHNLS NAVAAYTLAK KLGIKEKLIL SAIKKYKGAW RRMEYRGRFE ILDSRFKIPV
FDDYAHHPTE IKATLAAFXM TRIA
//
