ID A0A101HUA8_9BACT Unreviewed; 412 AA.
AC A0A101HUA8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamyl-2, 6-diaminopimelate/D-alanyl-D-alanyl ligase {ECO:0000313|EMBL:KUK83223.1};
DE EC=6.3.2.10 {ECO:0000313|EMBL:KUK83223.1};
GN ORFNames=XD98_0398 {ECO:0000313|EMBL:KUK83223.1};
OS Microgenomates bacterium 39_6.
OC Bacteria; Candidatus Microgenomates.
OX NCBI_TaxID=1641391 {ECO:0000313|EMBL:KUK83223.1, ECO:0000313|Proteomes:UP000053541};
RN [1] {ECO:0000313|Proteomes:UP000053541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(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:KUK83223.1}.
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DR EMBL; LGGT01000053; KUK83223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101HUA8; -.
DR PATRIC; fig|1641391.3.peg.389; -.
DR Proteomes; UP000053541; 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; 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:KUK83223.1}.
FT DOMAIN 32..224
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 245..319
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 412 AA; 46201 MW; AB84050CF0767C37 CRC64;
MIRLLKTFFH FVRRQLAKIW LRLHPQVKII AITGSYGKTN TSRAVEAVLK NHLETIVTDT
NLDTTYNLPI TLLKINKKTQ IAILEYCIDK KGEMEQHLNL VKPDIAIITG ITPVHSEKNM
LGSIKGIIEE KGKLLEALPK GGRAILNFDD PRVVKMAQKA PCPIISYGKK KTFDFYFDKA
TVTKRGTIFW AHFKKGNKKI SKKINLRLLG QHFAQEALAA LAIAKVLNID PNRAISSLEK
LSPLPGRMSL ENGPNGSLLI NDSLRANPAS TIAGLKTLST IEHSGKRIAV LGEMGELGQY
QEKEHYRVGQ FIGQLKNIDF LITLGPATKK IVQGAIEAGM NKNQIFYTKN HQETAEILKK
FLDSKTVWYL KGSLLKHVER IPMILEGKEV ACQKISCHNY YHCSKCKELN PG
//
