ID   RPO1C_METS5             Reviewed;         392 AA.
AC   A4YCR0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00411};
DE   AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000255|HAMAP-Rule:MF_00411};
GN   Name=rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
GN   Synonyms=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00411};
GN   OrderedLocusNames=Msed_0035;
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. Forms part of the jaw domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00411}.
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_00411};
CC   -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00411}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00411}.
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DR   EMBL; CP000682; ABP94212.1; -; Genomic_DNA.
DR   RefSeq; WP_011921181.1; NC_009440.1.
DR   AlphaFoldDB; A4YCR0; -.
DR   SMR; A4YCR0; -.
DR   STRING; 399549.Msed_0035; -.
DR   EnsemblBacteria; ABP94212; ABP94212; Msed_0035.
DR   GeneID; 5105174; -.
DR   GeneID; 59456533; -.
DR   KEGG; mse:Msed_0035; -.
DR   eggNOG; arCOG04256; Archaea.
DR   HOGENOM; CLU_037097_1_0_2; -.
DR   OMA; TPMMTVY; -.
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:UniProtKB-UniRule.
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   CDD; cd06528; RNAP_A; 1.
DR   HAMAP; MF_00411; RNApol_arch_Rpo1C; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR012757; RPO1C.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   TIGRFAMs; TIGR02389; RNA_pol_rpoA2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT   CHAIN           1..392
FT                   /note="DNA-directed RNA polymerase subunit Rpo1C"
FT                   /id="PRO_1000072276"
SQ   SEQUENCE   392 AA;  43742 MW;  499FEA62A627B753 CRC64;
     MINNTDNEYL EQKLSELSKK VPASIISKLR ESITNSPIEI TRDEIDKIIE IVMKDYLSSL
     VHPGEAIGVV AAQSIGEPGT QMTLRTFHFA GVRELNVTLG LPRLIEIVDA RKVPSTPMMT
     IYLNEEYAKD RDMALEVARR IEYTRVEHVV ETVNLDVGGM GIILKLDPVL LKDKGLSTED
     VEKVIKKLKM GDYRVENSDE YTIAIYFENM ETVTGLFKAR EKILSTKIKG VKGIKRAIIR
     KKGDEYVIIT DGSNLEGVLG VKGVDVSRIE TNNLHEVESV LGVEAARELI TREIKRVLEE
     QGLDVDIRHI ELVSDIMTRT GEVRQIGRHG VTGEKTSVLA RAAFEVTVKH LLDAAARGDM
     EEFKGVVENI IIGQPIKLGT GMVELLMRPA NR