RPO4_SULAC
ID RPO4_SULAC Reviewed; 114 AA.
AC Q4JB12;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
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, ECO:0000269|Ref.3};
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:15995215}; OrderedLocusNames=Saci_0625;
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 [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).
RN [2]
RP SUBUNIT.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=1729711; DOI=10.1073/pnas.89.1.407;
RA Klenk H.-P., Palm P., Lottspeich F., Zillig W.;
RT "Component H of the DNA-dependent RNA polymerases of Archaea is homologous
RT to a subunit shared by the three eucaryal nuclear RNA polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:407-410(1992).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MULTIPLE FORMS.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX DOI=10.1016/S0723-2020(11)80337-1;
RA Lanzendorfer M., Langer D., Hain J., Klenk H.-P., Holz I., Arnold-Ammer I.,
RA Zillig W.;
RT "Structure and Function of the DNA-Dependent RNA Polymerase of
RT Sulfolobus.";
RL Syst. Appl. Microbiol. 16:656-664(1994).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC This subunit is less well bound than the others (Ref.3). Probably not
CC involved in transcription inititation (Probable). {ECO:0000269|Ref.3,
CC ECO:0000305|Ref.3}.
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 ECO:0000269|Ref.3};
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:1729711, ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00864}.
CC -!- PTM: In purified enzyme appears as 5 forms, each differing by about 200
CC Da of a covalently bound, negatively charged residue. Not glycosylated.
CC {ECO:0000269|Ref.3}.
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; CP000077; AAY80017.1; -; Genomic_DNA.
DR RefSeq; WP_011277519.1; NC_007181.1.
DR PDB; 7OK0; EM; 2.90 A; F=1-114.
DR PDB; 7OQ4; EM; 3.27 A; F=1-114.
DR PDB; 7OQY; EM; 2.61 A; F=1-114.
DR PDBsum; 7OK0; -.
DR PDBsum; 7OQ4; -.
DR PDBsum; 7OQY; -.
DR SMR; Q4JB12; -.
DR STRING; 330779.Saci_0625; -.
DR EnsemblBacteria; AAY80017; AAY80017; Saci_0625.
DR GeneID; 3474211; -.
DR KEGG; sai:Saci_0625; -.
DR PATRIC; fig|330779.12.peg.604; -.
DR eggNOG; arCOG01016; Archaea.
DR HOGENOM; CLU_165894_0_0_2; -.
DR OMA; QIIEEDY; -.
DR Proteomes; UP000001018; 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; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
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..114
FT /note="DNA-directed RNA polymerase subunit Rpo4"
FT /id="PRO_0000453719"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:7OQ4"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:7OQY"
SQ SEQUENCE 114 AA; 13055 MW; FDCB0BA604D3B38D CRC64;
MSYSLKTIEE HFVPYSIAKK YIKELIDTGS SSNLIQKTFD YLNSISRCDE DSASKIMKEL
EEIVKREDVR AVLASICPTT VEEVRSVLVI DPSTIYSTEQ IQKIIEIIKK YVES
