TFS_SULAC
ID TFS_SULAC Reviewed; 111 AA.
AC Q07271; Q4JC89;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
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=Saci_0171;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=8502569; DOI=10.1093/nar/21.9.2251;
RA Langer D., Zillig W.;
RT "Putative tfIIs gene of Sulfolobus acidocaldarius encoding an archaeal
RT transcription elongation factor is situated directly downstream of the gene
RT for a small subunit of DNA-dependent RNA polymerase.";
RL Nucleic Acids Res. 21:2251-2251(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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=AAY79590.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X70805; CAA50073.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79590.1; ALT_INIT; Genomic_DNA.
DR PIR; S33694; S33694.
DR RefSeq; WP_015385375.1; NC_007181.1.
DR AlphaFoldDB; Q07271; -.
DR STRING; 330779.Saci_0171; -.
DR EnsemblBacteria; AAY79590; AAY79590; Saci_0171.
DR GeneID; 3473909; -.
DR KEGG; sai:Saci_0171; -.
DR PATRIC; fig|330779.12.peg.162; -.
DR eggNOG; arCOG00579; Archaea.
DR HOGENOM; CLU_093932_3_2_2; -.
DR BRENDA; 2.7.7.6; 6160.
DR Proteomes; UP000001018; 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; 2.
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..111
FT /note="Transcription factor S"
FT /id="PRO_0000121479"
FT ZN_FING 4..27
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 68..108
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT CONFLICT 28
FT /note="G -> A (in Ref. 1; CAA50073)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="E -> A (in Ref. 1; CAA50073)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="E -> A (in Ref. 1; CAA50073)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..62
FT /note="KT -> NP (in Ref. 1; CAA50073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 111 AA; 12694 MW; 555676F5A4D07357 CRC64;
MKFCPKCGSM MMPRKENGKT VYKCSKCGYI DTENQKEAKI TTVIKHSAKE KTLVLESDMP
KTGVQLTRGI SCPSCGNDEA YFWILQTRSA DEPATRFYKC TKCGKVWREY E
