AC MF_00870; DC Protein; auto TR HAMAP; MF_00870; -; 1; level=0 XX Names: FttA XX ID FTTA DE RecName: Full=Transcription termination factor FttA; DE EC=3.1.-.-; GN Name=fttA; XX CC -!- FUNCTION: Terminates transcription on the whole genome. Termination is CC linked to FttA-mediated RNA cleavage and does not require NTP CC hydrolysis. Cleaves endonucleolytically at the RNA exit channel of RNA CC polymerase (RNAP); the 5'-3' exonuclease activity of this protein CC degrades the nascent RNA released from RNAP. case and CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions, which are required for nuclease activity. end case CC -!- SUBUNIT: Homodimer. Interacts with RNA polymerase (RNAP), interacts CC with the Spt4-Spt5 complex. CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA- CC metabolizing metallo-beta-lactamase-like family. FttA subfamily. XX DR PROSITE; PS50084; KH_TYPE_1; 0-1; trigger=no DR Pfam; PF00753; Lactamase_B; 0-1; trigger=no DR Pfam; PF07521; RMMBL; 1; trigger=no DR Pfam; PF07650; KH_2; 0-1; trigger=no DR Pfam; PF10996; Beta-Casp; 1; trigger=no DR Pfam; PF16661; Lactamase_B_6; 0-1; trigger=no DR Pfam; PF17214; KH_7; 1; trigger=no DR NCBIfam; TIGR03675; arCOG00543; 1; trigger=no XX KW DNA-binding KW Endonuclease KW Exonuclease KW Hydrolase KW Nuclease KW RNA-binding KW Transcription regulation KW Transcription termination case or KW Zinc KW Metal-binding end case XX GO GO:0006353; P:DNA-templated transcription termination GO GO:0003723; F:RNA binding GO GO:0004521; F:RNA endonuclease activity GO GO:0004532; F:RNA exonuclease activity case or GO GO:0008270; F:zinc ion binding end case XX FT From: FTTA_METTH (O27271) FT REGION 3..70 FT /note="KHa" FT REGION 71..138 FT /note="KHb" FT REGION 179..383 FT /note="Metallo-beta-lactamase N-terminus" FT REGION 384..577 FT /note="Beta-Casp" FT REGION 578..636 FT /note="Metallo-beta-lactamase C-terminus" FT BINDING 242 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 244 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 246 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: D FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: H FT BINDING 329 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 352 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Group: 1; Condition: D FT BINDING 352 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: D FT BINDING 603 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: H XX Size: 634-651; Related: None; Template: Q5JH24; Q6LZD5; O27271; Q8PZ03; Q9V0P0; Scope: Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None # Revision 1.2 2024/03/04 //