ID   C0B861_9FIRM            Unreviewed;       256 AA.
AC   C0B861;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Mur ligase middle domain protein {ECO:0000313|EMBL:EEG90598.1};
GN   ORFNames=COPCOM_01335 {ECO:0000313|EMBL:EEG90598.1};
OS   Coprococcus comes ATCC 27758.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=470146 {ECO:0000313|EMBL:EEG90598.1, ECO:0000313|Proteomes:UP000003793};
RN   [1] {ECO:0000313|EMBL:EEG90598.1, ECO:0000313|Proteomes:UP000003793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27758 {ECO:0000313|EMBL:EEG90598.1,
RC   ECO:0000313|Proteomes:UP000003793};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG90598.1, ECO:0000313|Proteomes:UP000003793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27758 {ECO:0000313|EMBL:EEG90598.1,
RC   ECO:0000313|Proteomes:UP000003793};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Coprococcus comes (ATCC 27758).";
RL   Submitted (MAR-2009) 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:EEG90598.1}.
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DR   EMBL; ABVR01000038; EEG90598.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0B861; -.
DR   HOGENOM; CLU_031507_2_0_9; -.
DR   Proteomes; UP000003793; 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   Ligase {ECO:0000313|EMBL:EEG90598.1}.
FT   DOMAIN          27..75
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          110..235
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   256 AA;  27827 MW;  8A16CF875B2B3CC3 CRC64;
     MKNMTLKNIT AACHGTFHGD SSFLEKEITG VAIDSRKAAP GFLFVPLKGA RVDGHTFIPQ
     VMEQGALATL TEEDPSSLTC PCIHVESCEK ALRDIAAFYR MQLDIKVVGI TGSVGKTSTK
     ETIASVLSRK YNVLKTEGNF NNGIGLPLTI FNLTEEHEVA VLEMGIDHFG EMHELASISQ
     PDICVITNIG LAHMENLGSR DGILKAKTEV FDHLRPNASV ILNGDDDKLS TVAEVQGKSL
     FSSVFQTSWM PMQTES
//