TFS_METTH
ID TFS_METTH Reviewed; 104 AA.
AC O27369;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transcription factor S {ECO:0000250|UniProtKB:Q9P9I8};
DE AltName: Full=Transcription elongation factor IIS/RNA polymerase subunit homolog {ECO:0000250|UniProtKB:Q9P9I8};
DE Short=TFIIS/RPSU homolog {ECO:0000250|UniProtKB:Q9P9I8};
GN Name=tfs {ECO:0000250|UniProtKB:Q9P9I8}; OrderedLocusNames=MTH_1314;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Induces RNA cleavage activity in the RNA polymerase. In its
CC presence, the cleavage activity of the RNA polymerase truncates the RNA
CC back to position +15 in a stepwise manner by releasing mainly
CC dinucleotides from the 3'-end of the nascent RNA. The truncated RNAs
CC are able to continue elongation. Involved in transcriptional
CC proofreading and fidelity. Misincorporation of nucleotides during
CC elongation of transcription leads to arrested elongation complexes
CC which are rescued by TFS-promoted removal of a dinucleotide from the
CC 3'-end. TFS is able to induce a cleavage resynthesis cycle in stalled
CC elongation complexes (resulting from the next missing nucleotide or a
CC reduced incorporation rate of a wrong nucleotide) preventing
CC misincorporation and enabling proofreading in a post-incorporation
CC manner. Pausing of elongation complexes is the main determinant of TFS-
CC induced RNA cleavage. {ECO:0000250|UniProtKB:Q9P9I8}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
CC -!- CAUTION: More similar by sequence similarity to the eukaryotic RNA
CC polymerase subunits. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85792.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB85792.1; ALT_INIT; Genomic_DNA.
DR PIR; F69041; F69041.
DR RefSeq; WP_048061022.1; NC_000916.1.
DR AlphaFoldDB; O27369; -.
DR SMR; O27369; -.
DR STRING; 187420.MTH_1314; -.
DR EnsemblBacteria; AAB85792; AAB85792; MTH_1314.
DR GeneID; 1471031; -.
DR KEGG; mth:MTH_1314; -.
DR PATRIC; fig|187420.15.peg.1283; -.
DR HOGENOM; CLU_093932_3_2_2; -.
DR OMA; MVKFCPK; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR InterPro; IPR006288; TFS.
DR InterPro; IPR001222; Znf_TFIIS.
DR PANTHER; PTHR11239; PTHR11239; 1.
DR Pfam; PF02150; RNA_POL_M_15KD; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR SMART; SM00661; RPOL9; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR TIGRFAMs; TIGR01384; TFS_arch; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Metal-binding; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..104
FT /note="Transcription factor S"
FT /id="PRO_0000121482"
FT ZN_FING 4..22
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 61..101
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
SQ SEQUENCE 104 AA; 12356 MW; 36DACA10927C5CE8 CRC64;
MEFCPKCGAV MFPSEGKFKC QCGYEKDITD KLKDKYRVSE EVEAKETIIF TGDDVNTLPT
TRVECPKCGN MEAFWWLQQT RRADESETRF FRCTRCKHTW REYD
