RPO5_METS5
ID RPO5_METS5 Reviewed; 83 AA.
AC A4YCQ7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Msed_0032;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP94209.1; -; Genomic_DNA.
DR RefSeq; WP_011921178.1; NC_009440.1.
DR AlphaFoldDB; A4YCQ7; -.
DR SMR; A4YCQ7; -.
DR STRING; 399549.Msed_0032; -.
DR EnsemblBacteria; ABP94209; ABP94209; Msed_0032.
DR GeneID; 5105171; -.
DR GeneID; 59456536; -.
DR KEGG; mse:Msed_0032; -.
DR eggNOG; arCOG04258; Archaea.
DR HOGENOM; CLU_058320_4_0_2; -.
DR OMA; PKIYHDD; -.
DR Proteomes; UP000000242; 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_1000071009"
SQ SEQUENCE 83 AA; 9210 MW; A230D4FA4CCA8EFC CRC64;
MRSSSKKIDP SVHVLVPKHE VLSVEEAFKV LKELGIGPEQ LPWMRASDPM ARTINAKPGD
IVKITRKSPI VGELVVYRYV VSG