RPO6_SACS2
ID RPO6_SACS2 Reviewed; 95 AA.
AC Q97ZJ9;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo6 {ECO:0000255|HAMAP-Rule:MF_00192};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00192};
DE AltName: Full=DNA-directed RNA polymerase subunit K {ECO:0000255|HAMAP-Rule:MF_00192, ECO:0000303|PubMed:18235446};
GN Name=rpo6 {ECO:0000255|HAMAP-Rule:MF_00192}; Synonyms=rpoK;
GN OrderedLocusNames=SSO6768;
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:2PMZ, ECO:0007744|PDB:3HKZ}
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX, AND
RP 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_00192}.
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_00192};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:18235446}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00192}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00192}.
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DR EMBL; AE006641; AAK41189.1; -; Genomic_DNA.
DR PIR; F90241; F90241.
DR RefSeq; WP_009992332.1; NC_002754.1.
DR PDB; 2PMZ; X-ray; 3.40 A; K/W=1-95.
DR PDB; 3HKZ; X-ray; 3.40 A; K/U=1-95.
DR PDBsum; 2PMZ; -.
DR PDBsum; 3HKZ; -.
DR AlphaFoldDB; Q97ZJ9; -.
DR SMR; Q97ZJ9; -.
DR DIP; DIP-60642N; -.
DR IntAct; Q97ZJ9; 1.
DR STRING; 273057.SSO6768; -.
DR EnsemblBacteria; AAK41189; AAK41189; SSO6768.
DR GeneID; 44129837; -.
DR KEGG; sso:SSO6768; -.
DR PATRIC; fig|273057.12.peg.909; -.
DR eggNOG; arCOG01268; Archaea.
DR HOGENOM; CLU_112527_4_0_2; -.
DR InParanoid; Q97ZJ9; -.
DR OMA; KIGPPWL; -.
DR PhylomeDB; Q97ZJ9; -.
DR BRENDA; 2.7.7.6; 6163.
DR EvolutionaryTrace; Q97ZJ9; -.
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:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.940.10; -; 1.
DR HAMAP; MF_00192; RNApol_arch_Rpo6; 1.
DR InterPro; IPR020708; DNA-dir_RNA_polK_14-18kDa_CS.
DR InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR InterPro; IPR036161; RPB6/omega-like_sf.
DR InterPro; IPR006111; Rpo6/Rpb6.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF63562; SSF63562; 1.
DR PROSITE; PS01111; RNA_POL_K_14KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..95
FT /note="DNA-directed RNA polymerase subunit Rpo6"
FT /id="PRO_0000133823"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2PMZ"
SQ SEQUENCE 95 AA; 10858 MW; 2EA09FA9B1EAF55A CRC64;
MGLERDEILS QDLHFNEVFI SLWQNRLTRY EIARVISARA LQLAMGAPAL IDINNLSSTD
VISIAEEEFR RGVLPITIRR RLPNGKIILL SLRKS
