ID A0A1J4WNZ0_9BACT Unreviewed; 424 AA.
AC A0A1J4WNZ0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUJ45_01650 {ECO:0000313|EMBL:OIO50930.1};
OS Parcubacteria group bacterium CG1_02_50_68.
OC Bacteria.
OX NCBI_TaxID=1805312 {ECO:0000313|EMBL:OIO50930.1, ECO:0000313|Proteomes:UP000182181};
RN [1] {ECO:0000313|EMBL:OIO50930.1, ECO:0000313|Proteomes:UP000182181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_50_68 {ECO:0000313|EMBL:OIO50930.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO50930.1}.
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DR EMBL; MNWM01000023; OIO50930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4WNZ0; -.
DR STRING; 1805312.AUJ45_01650; -.
DR Proteomes; UP000182181; 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;
FT DOMAIN 31..212
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 424 AA; 46059 MW; F42D8C7553F6D055 CRC64;
MKNFLKSFIV FLLAFLARVV VRRYRPSIVM ISGSVGKTST KDAVAAVLSA RFLVRSSDKS
FNSEFGVPFT ILNVENPWGN PYAWFLVVKN ALALLLLPNH YPNMLVLEVG ADRPGDIARI
LRIATPDVVV ITRLPEIPVH VEAYTSPEAV HEEEFSPAYA LNATAPLIIP DDDPYVLICT
KRTPARCISY GMTDGASVRI TDVDFYEVAG KVAGMQANVS IKGGQWSLVV KGSVGKTQLL
PCAAALATAL AFEVSLPEAL KALEKYKPPP GRGQLLSGKN NSIIIDDSYN ASPAAVEEAL
ATLKISPRAK RRIAVLGDML ELGRYSVMEH KRIGALARDS ADLVVAVGIR ARAFASVSGN
AEVMLFDNSQ VAAEALSDLV RADDVILVKG SQSIRTERIV EALLADPSDT SRLVRQEKEW
KRKM
//
