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   27-MAR-2024, entry version 126.
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; Thermoproteota; 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   PaxDb; 273057-SSO6768; -.
DR   EnsemblBacteria; AAK41189; AAK41189; SSO6768.
DR   GeneID; 72912660; -.
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   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:0006360; P:transcription by RNA polymerase I; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IBA:GO_Central.
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   PANTHER; PTHR47227; DNA-DIRECTED RNA POLYMERASE SUBUNIT K; 1.
DR   PANTHER; PTHR47227:SF5; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2; 1.
DR   Pfam; PF01192; RNA_pol_Rpb6; 1.
DR   SMART; SM01409; RNA_pol_Rpb6; 1.
DR   SUPFAM; SSF63562; RPB6/omega subunit-like; 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
//