ID   RPO11_METBF             Reviewed;          92 AA.
AC   Q46C10;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Mbar_A1637;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ70582.1; -; Genomic_DNA.
DR   RefSeq; WP_011306628.1; NC_007355.1.
DR   AlphaFoldDB; Q46C10; -.
DR   SMR; Q46C10; -.
DR   STRING; 269797.Mbar_A1637; -.
DR   EnsemblBacteria; AAZ70582; AAZ70582; Mbar_A1637.
DR   GeneID; 3627336; -.
DR   KEGG; mba:Mbar_A1637; -.
DR   eggNOG; arCOG04111; Archaea.
DR   HOGENOM; CLU_090381_5_3_2; -.
DR   OMA; SYDMKHV; -.
DR   OrthoDB; 129321at2157; -.
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_0000232468"
SQ   SEQUENCE   92 AA;  10420 MW;  6E8E1C7796E6B2F4 CRC64;
     MELNILSKTD NELEVKLKGE THTLLNILKD LLIKDQRVEI AFYDMKYVSI SDPILYIKTD
     GTNPIEVLKD AASQIISQCD EFTDVFSKAV NA