RPO6_SULAC
ID RPO6_SULAC Reviewed; 89 AA.
AC P39463; Q4J925;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
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, ECO:0000269|Ref.4};
DE AltName: Full=DNA-directed RNA polymerase subunit K {ECO:0000255|HAMAP-Rule:MF_00192};
GN Name=rpo6 {ECO:0000255|HAMAP-Rule:MF_00192};
GN Synonyms=rpoK {ECO:0000255|HAMAP-Rule:MF_00192, ECO:0000303|Ref.1};
GN OrderedLocusNames=Saci_1370;
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;
RA Langer D., Hain J., Thuriaux P., Zillig W.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
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_00192,
CC ECO:0000269|Ref.4}.
CC -!- FUNCTION: Reconstitution experiments show this subunit is required for
CC basic activity. {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_00192,
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_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; X80753; CAA56729.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80704.1; -; Genomic_DNA.
DR PIR; S47328; S47328.
DR RefSeq; WP_011278206.1; NC_007181.1.
DR PDB; 7OK0; EM; 2.90 A; K=1-89.
DR PDB; 7OQ4; EM; 3.27 A; K=1-89.
DR PDB; 7OQY; EM; 2.61 A; K=1-89.
DR PDBsum; 7OK0; -.
DR PDBsum; 7OQ4; -.
DR PDBsum; 7OQY; -.
DR AlphaFoldDB; P39463; -.
DR SMR; P39463; -.
DR STRING; 330779.Saci_1370; -.
DR EnsemblBacteria; AAY80704; AAY80704; Saci_1370.
DR GeneID; 3472935; -.
DR KEGG; sai:Saci_1370; -.
DR PATRIC; fig|330779.12.peg.1322; -.
DR eggNOG; arCOG01268; Archaea.
DR HOGENOM; CLU_112527_4_0_2; -.
DR OMA; KIGPPWL; -.
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:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
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 PIRSF; PIRSF000778; RpoK/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..89
FT /note="DNA-directed RNA polymerase subunit Rpo6"
FT /id="PRO_0000133822"
FT CONFLICT 34..47
FT /note="LSMGALPLIDTSNL -> YLWSLTTDTYFYP (in Ref. 1;
FT CAA56729)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="D -> A (in Ref. 1; CAA56729)"
FT /evidence="ECO:0000305"
FT CONFLICT 57..60
FT /note="EEEL -> RGI (in Ref. 1; CAA56729)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..89
FT /note="Missing (in Ref. 1; CAA56729)"
FT /evidence="ECO:0000305"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7OQ4"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:7OQY"
SQ SEQUENCE 89 AA; 10237 MW; 5F0C5179C26DBE00 CRC64;
MTIDKINEIF KENWKNKLTK YEIARIISAR ALQLSMGALP LIDTSNLKSD DVISIAEEEL
KRGVLPITIR RIYPNGQVEL ISVRKIENR
