ID   RPO11_METAC             Reviewed;          92 AA.
AC   Q8TSS4;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
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}; OrderedLocusNames=MA_0721;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM04161.1; -; Genomic_DNA.
DR   RefSeq; WP_011020766.1; NC_003552.1.
DR   AlphaFoldDB; Q8TSS4; -.
DR   SMR; Q8TSS4; -.
DR   STRING; 188937.MA_0721; -.
DR   EnsemblBacteria; AAM04161; AAM04161; MA_0721.
DR   GeneID; 1472613; -.
DR   KEGG; mac:MA_0721; -.
DR   HOGENOM; CLU_090381_5_3_2; -.
DR   InParanoid; Q8TSS4; -.
DR   OMA; SYDMKHV; -.
DR   OrthoDB; 129321at2157; -.
DR   PhylomeDB; Q8TSS4; -.
DR   Proteomes; UP000002487; 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..92
FT                   /note="DNA-directed RNA polymerase subunit Rpo11"
FT                   /id="PRO_0000149325"
SQ   SEQUENCE   92 AA;  10374 MW;  B87AE96EAE9EC783 CRC64;
     MELNILNKTN NELEVELRGE THTLLNLLKD LLIKDERVEA AFYDMKHVSI SDPILYIKTD
     GTDPILVLKE TAAIIIAQCD EFIDVFSKAA NA