ID A0A1F6HQE5_9BACT Unreviewed; 427 AA.
AC A0A1F6HQE5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Mur ligase central domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2776_00405 {ECO:0000313|EMBL:OGH12498.1};
OS Candidatus Levybacteria bacterium RIFCSPHIGHO2_01_FULL_40_10.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798593 {ECO:0000313|EMBL:OGH12498.1, ECO:0000313|Proteomes:UP000177290};
RN [1] {ECO:0000313|EMBL:OGH12498.1, ECO:0000313|Proteomes:UP000177290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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:OGH12498.1}.
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DR EMBL; MFNQ01000046; OGH12498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6HQE5; -.
DR STRING; 1798593.A2776_00405; -.
DR Proteomes; UP000177290; 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 41..229
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 266..331
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 427 AA; 48698 MW; A7B21659933FEF47 CRC64;
MEQRESLIKK IKGQLYFFVA GYFKIFAQIK LARWKPKVIV ITGSSGKTTT LNLVESQLKD
SAVYSHHANS SYGVPFNILG LERKTLKHME WFSLILLAPF RIFTGTPKQK IYVVEADCDR
PQEGIFLSTL LNPEVTIWLS STRTHSINFD SLVTDKKFPN VESAIAFEYS HFLEKTSNLV
IYNSDSDLIK NQLGRTQAKT TSISEKSLNS YEVSKNGTKF KINKKTYSFK FLLPKASFSS
VYASILLNEY LNVPIDESFG DFELPPGRSS IFKGIKTTTI IDSTYNTGFH AAAEILNMFR
KFPGSKKWVV IGDILEQGKE EREEHEKLAA EILKMDLDRI VLVGPRVIKY TEPVLSRKNA
KNVVSFENPK EVLDYLKANI EGGETILFKG ARFLEGVIEN LLENKSDISK LARREEVWDE
RRKKWGL
//
