ID K2B7H9_9BACT Unreviewed; 400 AA.
AC K2B7H9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase {ECO:0000313|EMBL:EKD58044.1};
DE EC=6.3.2.10 {ECO:0000313|EMBL:EKD58044.1};
GN Name=murF {ECO:0000313|EMBL:EKD58044.1};
GN ORFNames=ACD_57C00042G0009 {ECO:0000313|EMBL:EKD58044.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD58044.1};
RN [1] {ECO:0000313|EMBL:EKD58044.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD58044.1}.
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DR EMBL; AMFJ01024484; EKD58044.1; -; Genomic_DNA.
DR AlphaFoldDB; K2B7H9; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
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:EKD58044.1}.
FT DOMAIN 40..225
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 247..326
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 400 AA; 44155 MW; 041230548F27C5D7 CRC64;
MTNSDVYREV KTWKKPIHAS RTLLARNYLK LLPNLEIIGI TGSVGKTLTQ NAIFSVLSQK
YKVVVGSENL DPTFRIPQTI LASKPWHQKL ILEYGVEHPG DIGHYLNLVR PKIAVVTVIA
PTHIKYFRGI EGVFEEKVKL VKALGKDGHV VLNADDPFVV RMANETQAKV WWYGRKAKSG
VKISHFSQNL KGSKFRLHYN GQKASVSTKI IGKHQLTSAY AAATVGIICN LTLKQIAKGL
SGARPPEHRL NLIVTKNARI IDDTYNASPK AAIESVNTLL DLGKRQKKIA VFGEMKDLGK
FSQEAHELVG LKIAKSKIQS LVTIGKTAST IANVAQKNGF SGEITNLETT KDAIDKIKKI
KTANSLILVK GSRHAHLERI VYGLLGKSTQ VNCYHCGELE
//
