ID   RPO6_SACSH              Reviewed;          95 AA.
AC   B8YB61;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo6 {ECO:0000255|HAMAP-Rule:MF_00192, ECO:0000303|PubMed:19419240};
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};
GN   Name=rpo6 {ECO:0000255|HAMAP-Rule:MF_00192, ECO:0000303|PubMed:19419240};
GN   Synonyms=rpoK {ECO:0000255|HAMAP-Rule:MF_00192};
OS   Saccharolobus shibatae (Sulfolobus shibatae).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=2286;
RN   [1] {ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.52 ANGSTROMS)
RP   OF THE RNA POLYMERASE COMPLEX, SUBUNIT, AND NOMENCLATURE.
RC   STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX   PubMed=19419240; DOI=10.1371/journal.pbio.1000102;
RA   Korkhin Y., Unligil U.M., Littlefield O., Nelson P.J., Stuart D.I.,
RA   Sigler P.B., Bell S.D., Abrescia N.G.;
RT   "Evolution of complex RNA polymerases: the complete archaeal RNA polymerase
RT   structure.";
RL   PLoS Biol. 7:e1000102-e1000102(2009).
RN   [2] {ECO:0007744|PDB:2Y0S}
RP   X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX   PubMed=21265742; DOI=10.1042/bst0390025;
RA   Wojtas M., Peralta B., Ondiviela M., Mogni M., Bell S.D., Abrescia N.G.;
RT   "Archaeal RNA polymerase: the influence of the protruding stalk in crystal
RT   packing and preliminary biophysical analysis of the Rpo13 subunit.";
RL   Biochem. Soc. Trans. 39:25-30(2011).
RN   [3] {ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S}
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX WITH
RP   AND WITHOUT DNA, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX   PubMed=22848102; DOI=10.1093/nar/gks692;
RA   Wojtas M.N., Mogni M., Millet O., Bell S.D., Abrescia N.G.;
RT   "Structural and functional analyses of the interaction of archaeal RNA
RT   polymerase with DNA.";
RL   Nucleic Acids Res. 40:9941-9952(2012).
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:19419240, ECO:0000269|PubMed:21265742,
CC       ECO:0000269|PubMed:22848102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00192,
CC       ECO:0000269|PubMed:22848102}.
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; FJ515673; ACL36496.1; -; Genomic_DNA.
DR   PDB; 2WAQ; X-ray; 3.35 A; K=11-92.
DR   PDB; 2WB1; X-ray; 3.52 A; I/K=1-95.
DR   PDB; 2Y0S; X-ray; 3.80 A; I/K=1-95.
DR   PDB; 4AYB; X-ray; 3.20 A; K=1-95.
DR   PDB; 4V8S; X-ray; 4.32 A; AI/BK=1-95.
DR   PDBsum; 2WAQ; -.
DR   PDBsum; 2WB1; -.
DR   PDBsum; 2Y0S; -.
DR   PDBsum; 4AYB; -.
DR   PDBsum; 4V8S; -.
DR   SMR; B8YB61; -.
DR   BRENDA; 2.7.7.6; 6162.
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; Transcription; Transferase.
FT   CHAIN           1..95
FT                   /note="DNA-directed RNA polymerase subunit Rpo6"
FT                   /id="PRO_0000453798"
FT   HELIX           14..23
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   HELIX           29..44
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   HELIX           62..70
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:4AYB"
SQ   SEQUENCE   95 AA;  10716 MW;  DB397018285CE8D6 CRC64;
     MGLERDGILS QDLHFNEVFV SLWQNKLTRY EIARVISARA LQLAMGAPAL IDINNISSTD
     VISIAEEEFK RGVLPITIRR RLPNGKIILL SLRKS