ID B6GCY8_9ACTN Unreviewed; 263 AA.
AC B6GCY8;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Mur ligase middle domain protein {ECO:0000313|EMBL:EEA89853.1};
DE Flags: Fragment;
GN ORFNames=COLSTE_01966 {ECO:0000313|EMBL:EEA89853.1};
OS Collinsella stercoris DSM 13279.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=445975 {ECO:0000313|EMBL:EEA89853.1, ECO:0000313|Proteomes:UP000003560};
RN [1] {ECO:0000313|EMBL:EEA89853.1, ECO:0000313|Proteomes:UP000003560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA89853.1,
RC ECO:0000313|Proteomes:UP000003560};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Collinsella stercoris (DSM 13279).";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEA89853.1, ECO:0000313|Proteomes:UP000003560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA89853.1,
RC ECO:0000313|Proteomes:UP000003560};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) 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:EEA89853.1}.
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DR EMBL; ABXJ01000114; EEA89853.1; -; Genomic_DNA.
DR AlphaFoldDB; B6GCY8; -.
DR STRING; 445975.COLSTE_01966; -.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_1059593_0_0_11; -.
DR Proteomes; UP000003560; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR005762; MurD.
DR PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EEA89853.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003560}.
FT DOMAIN 115..250
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT NON_TER 263
FT /evidence="ECO:0000313|EMBL:EEA89853.1"
SQ SEQUENCE 263 AA; 28368 MW; D83FFF3769CACC2A CRC64;
MPLPQRFSLL VLGQGSTGLE VVSWAVDHLG DRVTSVTVYG GAQSAPTERT RELEGAGVRF
AYGTEDIEGA YDICVASPGI SEFSEFFRNA SAACGEIMGE PEFAWRLSPE RWCAITGTNG
KTTVTSLTNE LLRASGLASV AVGNIGNAAI HEVDRRAEGE WFVAELSSYQ IATTAELHPR
VAILLNITPD HLAWHRTHEN YALAKIDLFR NMDESDLAIV NVEDEGIAAF ADRVYVPGRR
VLKLGLADAG GAHAAFVRDG HLV
//