ID   RPO5_HYPBU              Reviewed;          83 AA.
AC   A2BN32;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo5 {ECO:0000255|HAMAP-Rule:MF_00025};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00025};
DE   AltName: Full=DNA-directed RNA polymerase subunit H {ECO:0000255|HAMAP-Rule:MF_00025};
GN   Name=rpo5 {ECO:0000255|HAMAP-Rule:MF_00025};
GN   Synonyms=rpoH {ECO:0000255|HAMAP-Rule:MF_00025};
GN   OrderedLocusNames=Hbut_1572;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. {ECO:0000255|HAMAP-Rule:MF_00025}.
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_00025};
CC   -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00025}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00025}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_00025}.
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DR   EMBL; CP000493; ABM81393.1; -; Genomic_DNA.
DR   RefSeq; WP_011822711.1; NC_008818.1.
DR   AlphaFoldDB; A2BN32; -.
DR   SMR; A2BN32; -.
DR   STRING; 415426.Hbut_1572; -.
DR   EnsemblBacteria; ABM81393; ABM81393; Hbut_1572.
DR   GeneID; 4782374; -.
DR   KEGG; hbu:Hbut_1572; -.
DR   eggNOG; arCOG04258; Archaea.
DR   HOGENOM; CLU_058320_4_0_2; -.
DR   OMA; PKIYHDD; -.
DR   OrthoDB; 123463at2157; -.
DR   Proteomes; UP000002593; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.940.20; -; 1.
DR   HAMAP; MF_00025; RNApol_Rpo5_RPB5; 1.
DR   InterPro; IPR014381; Arch_Rpo5/euc_Rpb5.
DR   InterPro; IPR000783; RNA_pol_subH/Rpb5_C.
DR   InterPro; IPR020608; RNA_pol_subH/Rpb5_CS.
DR   InterPro; IPR035913; RPB5-like_sf.
DR   PANTHER; PTHR10535; PTHR10535; 1.
DR   Pfam; PF01191; RNA_pol_Rpb5_C; 1.
DR   SUPFAM; SSF55287; SSF55287; 1.
DR   PROSITE; PS01110; RNA_POL_H_23KD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..83
FT                   /note="DNA-directed RNA polymerase subunit Rpo5"
FT                   /id="PRO_1000074385"
SQ   SEQUENCE   83 AA;  9473 MW;  3E06F36D5AA58218 CRC64;
     MARQKKKFNI LEHELVPKHE VVPPEEAARI IRELGVRPEQ LPWLRATDPV ARAIGAKPGD
     IVRIYRKSPT AGEVVVYRYV VGY