TFS4_SACS2
ID TFS4_SACS2 Reviewed; 92 AA.
AC Q97X43;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Transcription factor S4 {ECO:0000303|PubMed:29203770};
DE Short=TFS4 {ECO:0000303|PubMed:29203770};
GN Name=tfs4 {ECO:0000303|PubMed:29203770};
GN Synonyms=rpoM-2 {ECO:0000303|PubMed:11427726}; OrderedLocusNames=SSO9221;
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 INDUCTION BY VIRUS.
RC STRAIN=2-2-12;
RX PubMed=18337566; DOI=10.1128/jvi.02583-07;
RA Ortmann A.C., Brumfield S.K., Walther J., McInnerney K., Brouns S.J.,
RA van de Werken H.J., Bothner B., Douglas T., van de Oost J., Young M.J.;
RT "Transcriptome analysis of infection of the archaeon Sulfolobus
RT solfataricus with Sulfolobus turreted icosahedral virus.";
RL J. Virol. 82:4874-4883(2008).
RN [3]
RP FUNCTION, PROBABLE COFACTOR, SUBUNIT, INDUCTION BY VIRUS, DOMAIN, ACTIVE
RP SITE, AND MUTAGENESIS OF 72-ILE--LYS-78; 76-LYS--LYS-78; 76-LYS-LYS-77;
RP LYS-76; 77-LYS-LYS-78; LYS-77 AND LYS-78.
RC STRAIN=2-2-12, and 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: A potent inhibitor of RNA polymerase (RNAP). Destabilizes the
CC transcription pre-initiation complex of TBP, TFB, DNA and RNAP,
CC inhibits abortive transcription initiation, productive initiation and
CC transcription elongation. Overexpression of TFS1-tip4 (TFS1 with the
CC active tip of this protein, phenocopies this protein) in
CC S.acidocaldarius MW001 leads to severe growth inhibition
CC (PubMed:29203770). May play a role in viral defense (Probable).
CC {ECO:0000269|PubMed:29203770, ECO:0000305|PubMed:29203770}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions. {ECO:0000305|PubMed:29203770};
CC -!- SUBUNIT: Interacts with RNA polymerase; probably competes with TFS1 for
CC the same binding site. {ECO:0000269|PubMed:29203770}.
CC -!- INDUCTION: At least 4-fold induced following infection by Sulfolobus
CC turreted icosahedral virus 1 (STIV-1) in strain 2-2-12
CC (PubMed:18337566). Undetected in non-infected cells. Induced following
CC STIV-1 infection, protein is detectable by 12 hours post-infection
CC (p.i.) and increases until at least 24 hours p.i. in strain 2-2-12 (at
CC protein level) (PubMed:29203770). {ECO:0000269|PubMed:18337566,
CC ECO:0000269|PubMed:29203770}.
CC -!- DOMAIN: Has 2 zinc-ribbon domains (N-ZR and C-ZR); functionally
CC important residues Lys-76, Lys-77 and Lys-78 are probably located at
CC the tip of a domain that extends from C-ZR into the RNAP active site.
CC The nature of these residues determines if the protein is involved in
CC stalled transcript cleavage and thus activation (Asp and Glu residues
CC in TFS1) or in RNAP inhibition (Lys or Arg residues in this protein
CC TFS4). Increasing numbers of Lys residues lead to an increased ability
CC to inhibit transcription. {ECO:0000269|PubMed:29203770,
CC ECO:0000305|PubMed:29203770}.
CC -!- MISCELLANEOUS: Strain 2-2-12 is a substrain of P2 that is highly
CC susceptible to infection by Sulfolobus turreted icosahedral virus 1
CC (STIV-1). {ECO:0000269|PubMed:18337566}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; AE006641; AAK42105.1; -; Genomic_DNA.
DR PIR; B90356; B90356.
DR PDB; 7OQY; EM; 2.61 A; Y=1-92.
DR PDBsum; 7OQY; -.
DR SMR; Q97X43; -.
DR STRING; 273057.SSO9221; -.
DR EnsemblBacteria; AAK42105; AAK42105; SSO9221.
DR KEGG; sso:SSO9221; -.
DR PATRIC; fig|273057.12.peg.1974; -.
DR eggNOG; arCOG00579; Archaea.
DR HOGENOM; CLU_2406498_0_0_2; -.
DR InParanoid; Q97X43; -.
DR OMA; KCGYSDH; -.
DR PhylomeDB; Q97X43; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR Pfam; PF02150; RNA_POL_M_15KD; 1.
DR SMART; SM00661; RPOL9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Metal-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..92
FT /note="Transcription factor S4"
FT /id="PRO_0000453930"
FT REGION 1..35
FT /note="N-ZR"
FT /evidence="ECO:0000305|PubMed:29203770"
FT REGION 53..92
FT /note="C-ZR"
FT /evidence="ECO:0000305|PubMed:29203770"
FT ACT_SITE 76
FT /evidence="ECO:0000269|PubMed:29203770"
FT ACT_SITE 77
FT /evidence="ECO:0000269|PubMed:29203770"
FT ACT_SITE 78
FT /evidence="ECO:0000269|PubMed:29203770"
FT BINDING 4
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|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 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:29203770"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:29203770"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:29203770"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:29203770"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:29203770"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:29203770"
FT MUTAGEN 72..78
FT /note="ILLNKKK->YFWILQTRRADEPPT: Does not inhibit RNAP
FT activity, has acquired transcript cleavage activity (TFS4-
FT tip1, with active tip of TFS1)."
FT /evidence="ECO:0000269|PubMed:29203770"
FT MUTAGEN 76..78
FT /note="KKK->AAA: No longer inhibits RNAP activity."
FT /evidence="ECO:0000269|PubMed:29203770"
FT MUTAGEN 76..78
FT /note="KKK->AKA: Mild decrease in RNAP activity."
FT /evidence="ECO:0000269|PubMed:29203770"
FT MUTAGEN 76..78
FT /note="KKK->RRR: Wild-type inhibition of RNAP activity."
FT /evidence="ECO:0000269|PubMed:29203770"
FT MUTAGEN 76..77
FT /note="KK->AA: Small decrease in RNAP activity."
FT /evidence="ECO:0000269|PubMed:29203770"
FT MUTAGEN 76
FT /note="K->A: Very small decrease in RNAP activity."
FT /evidence="ECO:0000269|PubMed:29203770"
FT MUTAGEN 77..78
FT /note="KK->AA: Medium decrease in RNAP activity."
FT /evidence="ECO:0000269|PubMed:29203770"
FT MUTAGEN 77
FT /note="K->A: Very small decrease in RNAP activity."
FT /evidence="ECO:0000269|PubMed:29203770"
FT MUTAGEN 78
FT /note="K->A: Mild decrease in RNAP activity."
FT /evidence="ECO:0000269|PubMed:29203770"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:7OQY"
SQ SEQUENCE 92 AA; 10403 MW; 88FB7493ECCC4416 CRC64;
MRFCPKCGSF LKVKGNKMVC SKCGYSDHDV EKVILKENVA HENDKTIIAD GETIEGRVAI
SLCPRCGSVR AILLNKKKRL YRCMTCNFVY NI
