RPO11_SULAC
ID RPO11_SULAC Reviewed; 90 AA.
AC P46217; Q4JC87;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 118.
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, ECO:0000269|Ref.4};
DE AltName: Full=DNA-directed RNA polymerase subunit L {ECO:0000255|HAMAP-Rule:MF_00261, ECO:0000303|PubMed:8502569};
GN Name=rpo11 {ECO:0000255|HAMAP-Rule:MF_00261};
GN Synonyms=rpoL {ECO:0000255|HAMAP-Rule:MF_00261,
GN ECO:0000303|PubMed:8502569}; OrderedLocusNames=Saci_0173;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=8502569; DOI=10.1093/nar/21.9.2251;
RA Langer D., Zillig W.;
RT "Putative tfIIs gene of Sulfolobus acidocaldarius encoding an archaeal
RT transcription elongation factor is situated directly downstream of the gene
RT for a small subunit of DNA-dependent RNA polymerase.";
RL Nucleic Acids Res. 21:2251-2251(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP SUBUNIT.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=1729711; DOI=10.1073/pnas.89.1.407;
RA Klenk H.-P., Palm P., Lottspeich F., Zillig W.;
RT "Component H of the DNA-dependent RNA polymerases of Archaea is homologous
RT to a subunit shared by the three eucaryal nuclear RNA polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:407-410(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX DOI=10.1016/S0723-2020(11)80337-1;
RA Lanzendorfer M., Langer D., Hain J., Klenk H.-P., Holz I., Arnold-Ammer I.,
RA Zillig W.;
RT "Structure and Function of the DNA-Dependent RNA Polymerase of
RT Sulfolobus.";
RL Syst. Appl. Microbiol. 16:656-664(1994).
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 ECO:0000269|Ref.4}.
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 ECO:0000269|Ref.4};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:1729711, ECO:0000269|Ref.4}.
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; X70805; CAA50072.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79592.1; -; Genomic_DNA.
DR PIR; S78047; S78047.
DR RefSeq; WP_011277093.1; NC_007181.1.
DR PDB; 7OK0; EM; 2.90 A; L=1-90.
DR PDB; 7OQ4; EM; 3.27 A; L=1-90.
DR PDB; 7OQY; EM; 2.61 A; L=1-90.
DR PDBsum; 7OK0; -.
DR PDBsum; 7OQ4; -.
DR PDBsum; 7OQY; -.
DR AlphaFoldDB; P46217; -.
DR SMR; P46217; -.
DR STRING; 330779.Saci_0173; -.
DR EnsemblBacteria; AAY79592; AAY79592; Saci_0173.
DR GeneID; 3473911; -.
DR KEGG; sai:Saci_0173; -.
DR PATRIC; fig|330779.12.peg.164; -.
DR eggNOG; arCOG04111; Archaea.
DR HOGENOM; CLU_090381_4_2_2; -.
DR OMA; PITMARK; -.
DR BRENDA; 2.7.7.6; 6160.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..90
FT /note="DNA-directed RNA polymerase subunit Rpo11"
FT /id="PRO_0000149338"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 65..87
FT /evidence="ECO:0007829|PDB:7OQY"
SQ SEQUENCE 90 AA; 10050 MW; 88785E0AAD696059 CRC64;
MEIKVIKEEQ NYLELQIDGE EHTIGNLLKG MLLKVPGVKF AAYSLPHPLI TSITIKILTD
GSISAREALI KAIELAENYA NLFIDEVKKI
