RPO11_SULIA
ID RPO11_SULIA Reviewed; 92 AA.
AC C3MZG6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=M1627_1927;
OS Sulfolobus islandicus (strain M.16.27).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.16.27;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001401; ACP55798.1; -; Genomic_DNA.
DR RefSeq; WP_012711784.1; NC_012632.1.
DR AlphaFoldDB; C3MZG6; -.
DR SMR; C3MZG6; -.
DR EnsemblBacteria; ACP55798; ACP55798; M1627_1927.
DR GeneID; 7812269; -.
DR GeneID; 7941876; -.
DR GeneID; 8761905; -.
DR KEGG; sim:M1627_1927; -.
DR HOGENOM; CLU_090381_5_1_2; -.
DR OMA; PITMARK; -.
DR Proteomes; UP000002307; 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 Transcription; Transferase.
FT CHAIN 1..92
FT /note="DNA-directed RNA polymerase subunit Rpo11"
FT /id="PRO_1000204668"
SQ SEQUENCE 92 AA; 10253 MW; F702C12488D31232 CRC64;
MEIKILKSER NYLELEIEGE DHTLGNLIAG TLRKISGVSF ASYYQPHPLT DKIIVKILTD
GSIAPKDALL KAIETVRVMA SHYIDEIKGL SK