ID A0A0G1D7H1_9BACT Unreviewed; 428 AA.
AC A0A0G1D7H1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase MurF {ECO:0000313|EMBL:KKS93632.1};
GN ORFNames=UV70_C0008G0031 {ECO:0000313|EMBL:KKS93632.1};
OS Parcubacteria group bacterium GW2011_GWA2_43_13.
OC Bacteria.
OX NCBI_TaxID=1618826 {ECO:0000313|EMBL:KKS93632.1, ECO:0000313|Proteomes:UP000034869};
RN [1] {ECO:0000313|EMBL:KKS93632.1, ECO:0000313|Proteomes:UP000034869}
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:KKS93632.1}.
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DR EMBL; LCFM01000008; KKS93632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1D7H1; -.
DR STRING; 1618826.UV70_C0008G0031; -.
DR PATRIC; fig|1618826.3.peg.590; -.
DR Proteomes; UP000034869; 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; 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; 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;
KW Ligase {ECO:0000313|EMBL:KKS93632.1}.
FT DOMAIN 101..248
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 270..353
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 428 AA; 46933 MW; 32F050F22D19C4C5 CRC64;
MKKIIYSIIR LLARGVLKKY KPDVVGITGS VGKTTTKDAI ALVMSGRFHI RASERSMNTE
VGLPLTVLGC ENPGKNVLAW LLVFWKGLWL LVHRDHEYPP ILVLEMAADK KGDIAYLCSI
TQPRIGVVTA LSEVHLAHFK SLEGVAKEKQ TLIASLPRNG WAVLNADDPR VVKMKELSDA
QCITFGIEEH ATVQAIDVSL RYKEGETFFD RINGLGFKVI YKGTATPILL SQSVGYHHVY
TALAACAVGT LFDMNPLEIG ERLGLLAPGP GRLRVLKGIN HSVLLDDSYN SSPLALERAL
DTLCDLNDPQ GNGHRRIAVL ADMLDLGKAS QEAHEVIGRK IAGLPIDQLV TIGHDSMFIA
EAAKNDGMDA AKLIHFDDMK SAEAYLKENI QEEDILLVKG SRGIHLEALV EKIIDEPHRG
RELLVSGH
//
