RPO11_SACS2
ID RPO11_SACS2 Reviewed; 92 AA.
AC Q980K0;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
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, ECO:0000303|PubMed:18235446};
GN Name=rpo11 {ECO:0000255|HAMAP-Rule:MF_00261};
GN Synonyms=rpoL {ECO:0000255|HAMAP-Rule:MF_00261,
GN ECO:0000303|PubMed:11427726}; OrderedLocusNames=SSO5577;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2] {ECO:0007744|PDB:2PA8, ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX, X-RAY
RP CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH RPO3, AND SUBUNIT.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=18235446; DOI=10.1038/nature06530;
RA Hirata A., Klein B.J., Murakami K.S.;
RT "The X-ray crystal structure of RNA polymerase from Archaea.";
RL Nature 451:851-854(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 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:18235446}.
CC -!- INTERACTION:
CC Q980K0; P95989: rpo3; NbExp=2; IntAct=EBI-9022031, EBI-9022065;
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; AE006641; AAK40631.1; -; Genomic_DNA.
DR PIR; H90171; H90171.
DR RefSeq; WP_009990580.1; NC_002754.1.
DR PDB; 2PA8; X-ray; 1.76 A; L=1-92.
DR PDB; 2PMZ; X-ray; 3.40 A; L/X=1-92.
DR PDB; 3HKZ; X-ray; 3.40 A; L/V=1-92.
DR PDBsum; 2PA8; -.
DR PDBsum; 2PMZ; -.
DR PDBsum; 3HKZ; -.
DR AlphaFoldDB; Q980K0; -.
DR SMR; Q980K0; -.
DR DIP; DIP-60647N; -.
DR IntAct; Q980K0; 2.
DR STRING; 273057.SSO5577; -.
DR EnsemblBacteria; AAK40631; AAK40631; SSO5577.
DR GeneID; 44129266; -.
DR KEGG; sso:SSO5577; -.
DR PATRIC; fig|273057.12.peg.286; -.
DR eggNOG; arCOG04111; Archaea.
DR HOGENOM; CLU_090381_5_1_2; -.
DR InParanoid; Q980K0; -.
DR OMA; PITMARK; -.
DR PhylomeDB; Q980K0; -.
DR BRENDA; 2.7.7.6; 6163.
DR EvolutionaryTrace; Q980K0; -.
DR Proteomes; UP000001974; 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; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..92
FT /note="DNA-directed RNA polymerase subunit Rpo11"
FT /id="PRO_0000149339"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:2PA8"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:2PA8"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:2PA8"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2PA8"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:2PA8"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2PA8"
FT HELIX 65..91
FT /evidence="ECO:0007829|PDB:2PA8"
SQ SEQUENCE 92 AA; 10285 MW; B8F3DDA07598088C CRC64;
MEIRILKSES NYLELEIEGE DHTLGNLIAG TLRRISGVSF ASYYQPHPLS DKIIVKILTD
GSITPKDALL KAIENIRGMT SHYIDEIKGL TK
