RPO4_SACSH
ID RPO4_SACSH Reviewed; 113 AA.
AC B8YB58;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo4 {ECO:0000255|HAMAP-Rule:MF_00864, ECO:0000303|PubMed:19419240};
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, ECO:0000303|PubMed:19419240};
GN Synonyms=rpoF {ECO:0000255|HAMAP-Rule:MF_00864};
OS Saccharolobus shibatae (Sulfolobus shibatae).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2286;
RN [1] {ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS)
RP OF THE RNA POLYMERASE COMPLEX, SUBUNIT, FUNCTION, AND NOMENCLATURE.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=19419240; DOI=10.1371/journal.pbio.1000102;
RA Korkhin Y., Unligil U.M., Littlefield O., Nelson P.J., Stuart D.I.,
RA Sigler P.B., Bell S.D., Abrescia N.G.;
RT "Evolution of complex RNA polymerases: the complete archaeal RNA polymerase
RT structure.";
RL PLoS Biol. 7:e1000102-e1000102(2009).
RN [2] {ECO:0007744|PDB:2Y0S}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX,
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=21265742; DOI=10.1042/bst0390025;
RA Wojtas M., Peralta B., Ondiviela M., Mogni M., Bell S.D., Abrescia N.G.;
RT "Archaeal RNA polymerase: the influence of the protruding stalk in crystal
RT packing and preliminary biophysical analysis of the Rpo13 subunit.";
RL Biochem. Soc. Trans. 39:25-30(2011).
RN [3] {ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX WITH
RP AND WITHOUT DNA, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=22848102; DOI=10.1093/nar/gks692;
RA Wojtas M.N., Mogni M., Millet O., Bell S.D., Abrescia N.G.;
RT "Structural and functional analyses of the interaction of archaeal RNA
RT polymerase with DNA.";
RL Nucleic Acids Res. 40:9941-9952(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates (Probable). The highly mobile Rpo4/Rpo7
CC heterodimer stalk is conditionally required for transcription
CC initiation (Probable). {ECO:0000305|PubMed:19419240,
CC ECO:0000305|PubMed:21265742, ECO:0000305|PubMed:22848102}.
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:19419240, ECO:0000269|PubMed:21265742,
CC ECO:0000269|PubMed:22848102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00864,
CC ECO:0000269|PubMed:22848102}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB4 RNA polymerase subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00864}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ515670; ACL36493.1; -; Genomic_DNA.
DR PDB; 2WAQ; X-ray; 3.35 A; F=1-113.
DR PDB; 2WB1; X-ray; 3.52 A; F/U=1-113.
DR PDB; 2Y0S; X-ray; 3.80 A; F/U=1-113.
DR PDB; 4AYB; X-ray; 3.20 A; F=1-113.
DR PDB; 4V8S; X-ray; 4.32 A; AU/BF=1-113.
DR PDBsum; 2WAQ; -.
DR PDBsum; 2WB1; -.
DR PDBsum; 2Y0S; -.
DR PDBsum; 4AYB; -.
DR PDBsum; 4V8S; -.
DR SMR; B8YB58; -.
DR GeneID; 7811830; -.
DR BRENDA; 2.7.7.6; 6162.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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; Transcription; Transferase.
FT CHAIN 1..113
FT /note="DNA-directed RNA polymerase subunit Rpo4"
FT /id="PRO_0000453812"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 20..24
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2WAQ"
FT TURN 85..90
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:4AYB"
SQ SEQUENCE 113 AA; 12808 MW; D85CC353E314271A CRC64;
MSSVYIVEEH YIPYSVAKKL LSDVIKSGSS SNLLQRTYDY LNSVEKCDAE SAQKVVEELS
SIISREDVRA VLASICPITP DEVRSILIMD SNRTYTSEDI QKIIDIIRKY IKS
