RPO4_SACS2
ID RPO4_SACS2 Reviewed; 113 AA.
AC Q7LXK4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo4 {ECO:0000255|HAMAP-Rule:MF_00864};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00864};
DE AltName: Full=DNA-directed RNA polymerase subunit F {ECO:0000255|HAMAP-Rule:MF_00864};
GN Name=rpo4 {ECO:0000255|HAMAP-Rule:MF_00864};
GN Synonyms=rpoF {ECO:0000255|HAMAP-Rule:MF_00864,
GN ECO:0000303|PubMed:11427726}; OrderedLocusNames=SSO0751;
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] {ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ}
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX, AND
RP SUBUNIT.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=18235446; DOI=10.1038/nature06530;
RA Hirata A., Klein B.J., Murakami K.S.;
RT "The X-ray crystal structure of RNA polymerase from Archaea.";
RL Nature 451:851-854(2008).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. This subunit is less well bound than the
CC others. {ECO:0000255|HAMAP-Rule:MF_00864}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00864};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex. Forms a stalk
CC with Rpo7 that extends from the main structure.
CC {ECO:0000269|PubMed:18235446}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00864}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB4 RNA polymerase subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00864}.
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DR EMBL; AE006641; AAK41046.1; -; Genomic_DNA.
DR PIR; G90223; G90223.
DR RefSeq; WP_009991330.1; NC_002754.1.
DR PDB; 2PMZ; X-ray; 3.40 A; F/U=1-113.
DR PDB; 3HKZ; X-ray; 3.40 A; F/R=1-113.
DR PDBsum; 2PMZ; -.
DR PDBsum; 3HKZ; -.
DR SMR; Q7LXK4; -.
DR DIP; DIP-60648N; -.
DR IntAct; Q7LXK4; 1.
DR STRING; 273057.SSO0751; -.
DR EnsemblBacteria; AAK41046; AAK41046; SSO0751.
DR GeneID; 44129746; -.
DR KEGG; sso:SSO0751; -.
DR PATRIC; fig|273057.12.peg.746; -.
DR eggNOG; arCOG01016; Archaea.
DR HOGENOM; CLU_165894_0_0_2; -.
DR InParanoid; Q7LXK4; -.
DR OMA; QIIEEDY; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR Gene3D; 1.10.150.80; -; 1.
DR HAMAP; MF_00864; RNApol_arch_Rpo4; 1.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR005574; Rpb4/RPC9.
DR InterPro; IPR010924; Rpo4.
DR PANTHER; PTHR39646; PTHR39646; 1.
DR Pfam; PF03874; RNA_pol_Rpb4; 1.
DR PIRSF; PIRSF005053; RNA_pol_F_arch; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..113
FT /note="DNA-directed RNA polymerase subunit Rpo4"
FT /id="PRO_0000453811"
SQ SEQUENCE 113 AA; 12811 MW; DB070B2E7E4843DC CRC64;
MSSVYIVEEH YIPYSVAKKL LTDVIRSGGS SNLLQRTYDY LNSVEKCDAE SAQKVIEELS
NIVSREDVRA ILASICPTTS DEVRSILVMD TNKTYTSEDI QKIIDIIRKY IKS