RPO8_SACSH
ID RPO8_SACSH Reviewed; 132 AA.
AC B8YB59;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo8 {ECO:0000255|HAMAP-Rule:MF_00866, ECO:0000303|PubMed:19419240};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00866};
DE AltName: Full=DNA-directed RNA polymerase, subunit G {ECO:0000255|HAMAP-Rule:MF_00866};
DE AltName: Full=RNA polymerase subunit 8;
GN Name=rpo8 {ECO:0000255|HAMAP-Rule:MF_00866, ECO:0000303|PubMed:19419240};
GN Synonyms=rpoG {ECO:0000255|HAMAP-Rule:MF_00866};
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 (3.35 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_00866}.
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 -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex. Interacts with
CC Rpo1N on the periphery of the clamp head. {ECO:0000269|PubMed:19419240,
CC ECO:0000269|PubMed:21265742, ECO:0000269|PubMed:22848102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00866,
CC ECO:0000269|PubMed:22848102}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo8 RNA polymerase subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_00866}.
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DR EMBL; FJ515671; ACL36494.1; -; Genomic_DNA.
DR PDB; 2WAQ; X-ray; 3.35 A; G=1-132.
DR PDB; 2WB1; X-ray; 3.52 A; G/V=1-132.
DR PDB; 2Y0S; X-ray; 3.80 A; G/V=1-132.
DR PDB; 4AYB; X-ray; 3.20 A; G=1-132.
DR PDB; 4V8S; X-ray; 4.32 A; AV/BG=1-132.
DR PDBsum; 2WAQ; -.
DR PDBsum; 2WB1; -.
DR PDBsum; 2Y0S; -.
DR PDBsum; 4AYB; -.
DR PDBsum; 4V8S; -.
DR SMR; B8YB59; -.
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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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; Transcription; Transferase.
FT CHAIN 1..132
FT /note="DNA-directed RNA polymerase subunit Rpo8"
FT /id="PRO_0000453880"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 33..44
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:4AYB"
SQ SEQUENCE 132 AA; 15120 MW; 0FB1C2BE0C087F14 CRC64;
MMESKAQEII LSCEINSIER GSLKNLSIIH MSCNDFNISF DIIDSINIFS QKEKVKAFIS
KNRLSYTNDD FCGHGYIVTE LKDSSSNNGN RYITIISLFG LLVKIISNKE SFLKIHQLNV
MDHIYFCVKK NT
