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Database: UniProt
Entry: A0A0G1GTI0_9BACT
LinkDB: A0A0G1GTI0_9BACT
Original site: A0A0G1GTI0_9BACT 
ID   A0A0G1GTI0_9BACT        Unreviewed;       432 AA.
AC   A0A0G1GTI0;
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-acetylmuramoylalanyl-D-glutamyl-2, 6-diaminopimelate-D-alanyl-D-alanyl ligase, UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase {ECO:0000313|EMBL:KKT01959.1};
DE            EC=6.3.2.10 {ECO:0000313|EMBL:KKT01959.1};
GN   ORFNames=UV80_C0007G0073 {ECO:0000313|EMBL:KKT01959.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWF2_43_17.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619068 {ECO:0000313|EMBL:KKT01959.1, ECO:0000313|Proteomes:UP000034674};
RN   [1] {ECO:0000313|EMBL:KKT01959.1, ECO:0000313|Proteomes:UP000034674}
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:KKT01959.1}.
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DR   EMBL; LCFW01000007; KKT01959.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1GTI0; -.
DR   STRING; 1619068.UV80_C0007G0073; -.
DR   PATRIC; fig|1619068.3.peg.922; -.
DR   Proteomes; UP000034674; Unassembled WGS sequence.
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; 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; 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:KKT01959.1}.
FT   DOMAIN          37..249
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   432 AA;  47724 MW;  66A6802728C1FABA CRC64;
     MNFAAKIKTG VRGYVVSYLY ALAKRRLEKL QAEVIGITGS VGKTSTKDAI YCVLARRYTV
     LRNKKSFNTE LGVPLGILEQ ESGFSSPFAW LEILWKAFKV AIFDKTSYGK VVLEMGVDKP
     GDMDQLLKLV KPTIGVMTAI KAVHLAEGQF QNLEEILKEK AKLIKNIGKT GWAILNADDH
     YLSLLASQLE ANVITFGMNE KANIRAVNVA SSEEGLKFDL AFDDKNFSVH LPHLIGKHHV
     YVLLPAIAIG FLNSFKWETI KAGLEDFRLP PGRLTLLPGI NKTLVIDGSY NASPSTMIVS
     LEVLSEMKPK GVGRKIAALG SMNELGDFAD SEHRKIGKEV LKHADMLVTV GDLAQLYAEE
     ALKGGMDKGS VWSFKNSKEA GEFLKGKLRP GDLILAKGSQ NNVRMEYLVK EIMLEPEKAK
     DLLVRQETAW NI
//
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