RPO8_SULAC
ID RPO8_SULAC Reviewed; 121 AA.
AC Q4JAY4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo8 {ECO:0000255|HAMAP-Rule:MF_00866};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00866, ECO:0000269|Ref.2};
DE AltName: Full=DNA-directed RNA polymerase, subunit G {ECO:0000255|HAMAP-Rule:MF_00866, ECO:0000303|PubMed:1729711};
GN Name=rpo8 {ECO:0000255|HAMAP-Rule:MF_00866};
GN Synonyms=rpoG {ECO:0000255|HAMAP-Rule:MF_00866};
GN OrderedLocusNames=Saci_0661;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP AND PHOSPHORYLATION.
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).
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).
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_00866,
CC ECO:0000269|Ref.2}.
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_00866,
CC ECO:0000269|Ref.2};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:1729711, ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00866}.
CC -!- PTM: This subunit is phosphorylated. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo8 RNA polymerase subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY80045.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000077; AAY80045.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011277547.1; NC_007181.1.
DR PDB; 7OK0; EM; 2.90 A; G=1-121.
DR PDB; 7OQ4; EM; 3.27 A; G=1-121.
DR PDB; 7OQY; EM; 2.61 A; G=1-121.
DR PDBsum; 7OK0; -.
DR PDBsum; 7OQ4; -.
DR PDBsum; 7OQY; -.
DR SMR; Q4JAY4; -.
DR STRING; 330779.Saci_0661; -.
DR EnsemblBacteria; AAY80045; AAY80045; Saci_0661.
DR GeneID; 3473232; -.
DR KEGG; sai:Saci_0661; -.
DR PATRIC; fig|330779.12.peg.631; -.
DR eggNOG; arCOG04271; Archaea.
DR HOGENOM; CLU_136588_0_0_2; -.
DR OMA; IMDHIYF; -.
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:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00866; RNApol_arch_Rpo8; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR031555; RNA_pol_Rpo8.
DR Pfam; PF16992; RNA_pol_RpbG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome; Transcription;
KW Transferase.
FT CHAIN 1..121
FT /note="DNA-directed RNA polymerase subunit Rpo8"
FT /id="PRO_0000453720"
FT CONFLICT 82
FT /note="F -> L (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..100
FT /note="SKNG -> AKMR (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="D -> V (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 115..121
FT /note="YCVKKKA -> MRKKSI (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 64..76
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:7OQ4"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:7OQY"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:7OQY"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:7OQY"
SQ SEQUENCE 121 AA; 14054 MW; A670ADE4E06AA71A CRC64;
MMQGTCKISS IEKGALKNLY VVKMDCDNDL KIEFDITKEL SIFSKDEEVT FIISREKPEY
SEKDFCAHGY LFLERQQEDG SFIDEISLYG LIVKILSKNG LINSKLFKMM DHVYYCVKKK
A
