ID   RPO11_METS5             Reviewed;          90 AA.
AC   A4YHV0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo11 {ECO:0000255|HAMAP-Rule:MF_00261};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00261};
DE   AltName: Full=DNA-directed RNA polymerase subunit L {ECO:0000255|HAMAP-Rule:MF_00261};
GN   Name=rpo11 {ECO:0000255|HAMAP-Rule:MF_00261};
GN   Synonyms=rpoL {ECO:0000255|HAMAP-Rule:MF_00261};
GN   OrderedLocusNames=Msed_1862;
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_00261}.
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_00261};
CC   -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00261}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00261}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA
CC       polymerase subunit family. {ECO:0000255|HAMAP-Rule:MF_00261}.
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DR   EMBL; CP000682; ABP96002.1; -; Genomic_DNA.
DR   RefSeq; WP_012021789.1; NC_009440.1.
DR   AlphaFoldDB; A4YHV0; -.
DR   SMR; A4YHV0; -.
DR   STRING; 399549.Msed_1862; -.
DR   EnsemblBacteria; ABP96002; ABP96002; Msed_1862.
DR   GeneID; 5104130; -.
DR   GeneID; 59457009; -.
DR   KEGG; mse:Msed_1862; -.
DR   eggNOG; arCOG04111; Archaea.
DR   HOGENOM; CLU_090381_5_3_2; -.
DR   OMA; PITMARK; -.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1360.10; -; 1.
DR   HAMAP; MF_00261; RNApol_arch_Rpo11; 1.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR009025; RBP11-like_dimer.
DR   InterPro; IPR008193; RNA_pol_Rpb11_13-16kDa_CS.
DR   InterPro; IPR022905; Rpo11.
DR   Pfam; PF13656; RNA_pol_L_2; 1.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   PROSITE; PS01154; RNA_POL_L_13KD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..90
FT                   /note="DNA-directed RNA polymerase subunit Rpo11"
FT                   /id="PRO_1000071889"
SQ   SEQUENCE   90 AA;  10216 MW;  E1041B24C532AAA8 CRC64;
     MEIAVEREEE NYLELRIQGE DHTLGNLIAG RLRSVKGVIL ATYYLPHPLK DELVIKIKTD
     GTISPREALN RAIEDVKVLG ESFLDELEQV