TFS1_SACS2
ID TFS1_SACS2 Reviewed; 114 AA.
AC Q980K2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transcription factor S1 {ECO:0000303|PubMed:29203770};
DE Short=TFS1 {ECO:0000303|PubMed:29203770};
DE AltName: Full=Transcript cleavage factor TFS1 {ECO:0000303|PubMed:29203770};
GN Name=tfs1 {ECO:0000303|PubMed:11427726};
GN Synonyms=rpoM-1 {ECO:0000303|PubMed:11427726}; OrderedLocusNames=SSO0291;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION IN TRANSCRIPT CLEAVAGE, PROBABLE COFACTOR, SUBUNIT, DOMAIN, ACTIVE
RP SITE, AND MUTAGENESIS OF 84-TYR--THR-98 AND 94-ASP-GLU-95.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=29203770; DOI=10.1038/s41467-017-02081-3;
RA Fouqueau T., Blombach F., Hartman R., Cheung A.C.M., Young M.J., Werner F.;
RT "The transcript cleavage factor paralogue TFS4 is a potent RNA polymerase
RT inhibitor.";
RL Nat. Commun. 8:1914-1914(2017).
CC -!- FUNCTION: Induces RNA cleavage activity in the RNA polymerase. Induces
CC rapid cleavage of a stalled transcription elongation complex with a 2-
CC nucleotide reduction at the 3' end of the nascent RNA. Truncated RNA is
CC able to resume elongation. During transcription elongation it enhances
CC processivity (PubMed:29203770). 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. TFS1 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 (By similarity). {ECO:0000250|UniProtKB:Q9P9I8,
CC ECO:0000269|PubMed:29203770}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:29203770};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000305|PubMed:29203770};
CC -!- SUBUNIT: Interacts with RNA polymerase; probably competes with TFS4 for
CC the same binding site. {ECO:0000269|PubMed:29203770}.
CC -!- DOMAIN: Has 2 zinc-ribbon domains (N-ZR and C-ZR); functionally
CC important residues Asp-94 and Glu-95 are probably located at the tip of
CC a domain that extends from C-ZR into the RNAP active site. The nature
CC of these residues determines if the protein is involved in stalled
CC transcript cleavage and thus activation (Asp and Glu residues in this
CC protein, TFS1) or in RNAP inhibition (Lys residues in TFS4).
CC {ECO:0000269|PubMed:29203770, ECO:0000305|PubMed:29203770}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; AE006641; AAK40629.1; -; Genomic_DNA.
DR PIR; F90171; F90171.
DR SMR; Q980K2; -.
DR STRING; 273057.SSO0291; -.
DR EnsemblBacteria; AAK40629; AAK40629; SSO0291.
DR KEGG; sso:SSO0291; -.
DR PATRIC; fig|273057.12.peg.284; -.
DR eggNOG; arCOG00579; Archaea.
DR HOGENOM; CLU_093932_3_2_2; -.
DR InParanoid; Q980K2; -.
DR OMA; MVKFCPK; -.
DR PhylomeDB; Q980K2; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA: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 1: Evidence at protein level;
KW Activator; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..114
FT /note="Transcription factor S1"
FT /id="PRO_0000453929"
FT ZN_FING 71..111
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT REGION 1..43
FT /note="N-ZR"
FT /evidence="ECO:0000305|PubMed:29203770"
FT REGION 63..114
FT /note="C-ZR"
FT /evidence="ECO:0000305|PubMed:29203770"
FT ACT_SITE 94
FT /evidence="ECO:0000269|PubMed:29203770"
FT ACT_SITE 95
FT /evidence="ECO:0000269|PubMed:29203770"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:29203770"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:29203770"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:29203770"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:29203770"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000305|PubMed:29203770"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000305|PubMed:29203770"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000305|PubMed:29203770"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000305|PubMed:29203770"
FT MUTAGEN 84..98
FT /note="YFWILQTRRADEPPT->ILLNKKK: Inhibits RNAP activity,
FT destabilizes pre-initiation complex and inhibits
FT transcription initiation (TFS1-tip4, with active tip of
FT TFS4)."
FT /evidence="ECO:0000269|PubMed:29203770"
FT MUTAGEN 94..95
FT /note="DE->AA: Loss of RNA cleavage activity, reduces
FT transcription processivity."
FT /evidence="ECO:0000269|PubMed:29203770"
SQ SEQUENCE 114 AA; 13206 MW; 468A4680CA4AEED2 CRC64;
MIVVKFCPKC NSMMVPKKSN GKNVYRCTKC GYEKEVPETT IVVTSKVKHS IKEKTLVLEE
EEMPSGAQKI KGVLCPSCKN DEAYFWILQT RRADEPPTRF YKCTKCGKVW REYE
