ID G5IG08_9CLOT Unreviewed; 156 AA.
AC G5IG08;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Mur ligase central domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9473_02436 {ECO:0000313|EMBL:EHI59577.1};
OS Hungatella hathewayi WAL-18680.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=742737 {ECO:0000313|EMBL:EHI59577.1, ECO:0000313|Proteomes:UP000005384};
RN [1] {ECO:0000313|EMBL:EHI59577.1, ECO:0000313|Proteomes:UP000005384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL-18680 {ECO:0000313|EMBL:EHI59577.1,
RC ECO:0000313|Proteomes:UP000005384};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA Molitoris D.R., Song M., Daigneault M., Allen-Vercoe E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium hathewayi WAL-18680.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHI59577.1}.
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DR EMBL; ADLN01000053; EHI59577.1; -; Genomic_DNA.
DR AlphaFoldDB; G5IG08; -.
DR PATRIC; fig|742737.3.peg.2456; -.
DR HOGENOM; CLU_031507_2_2_9; -.
DR Proteomes; UP000005384; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000713; Mur_ligase_N.
DR InterPro; IPR035911; MurE/MurF_N.
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; PF01225; Mur_ligase; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000005384}.
FT DOMAIN 26..98
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 113..150
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 156 AA; 17070 MW; C8F9D8B26AA50F89 CRC64;
MEEITVKEIV EASGGRLLCG RPETPVEHIS IDSRTMKGND LFVPLIGEKV DAHRFIMQAI
NAGAVAVFTS EHDQMEEEQS GGAAWIRVED TKKALQSVGA WYRSRLNLPL IGVTGSVGKT
TTREMISAAL SAGYRVYKTP GNHNSQVGVP THPRRR
//