RPO13_SULAC
ID RPO13_SULAC Reviewed; 105 AA.
AC Q4JAJ6;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo13 {ECO:0000305};
DE EC=2.7.7.6 {ECO:0000269|Ref.2};
DE AltName: Full=DNA-directed RNA polymerase subunit F {ECO:0000303|Ref.2};
GN Name=rpo13 {ECO:0000305};
GN OrderedLocusNames=Saci_0816 {ECO:0000312|EMBL:AAY80183.1};
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, AND
RP 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).
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 DNA-BINDING.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
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 catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates
CC (Ref.2). In vitro binds dsDNA but not ssDNA (PubMed:22848102).
CC {ECO:0000269|PubMed:22848102, 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:0000269|Ref.2};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase.
CC {ECO:0000269|PubMed:1729711, ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8YB65}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo13 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; CP000077; AAY80183.1; -; Genomic_DNA.
DR RefSeq; WP_011277685.1; NC_007181.1.
DR PDB; 7OK0; EM; 2.90 A; Q=1-105.
DR PDB; 7OQ4; EM; 3.27 A; Q=1-105.
DR PDB; 7OQY; EM; 2.61 A; Q=1-105.
DR PDBsum; 7OK0; -.
DR PDBsum; 7OQ4; -.
DR PDBsum; 7OQY; -.
DR SMR; Q4JAJ6; -.
DR STRING; 330779.Saci_0816; -.
DR EnsemblBacteria; AAY80183; AAY80183; Saci_0816.
DR GeneID; 3472652; -.
DR KEGG; sai:Saci_0816; -.
DR PATRIC; fig|330779.12.peg.780; -.
DR eggNOG; arCOG05938; Archaea.
DR HOGENOM; CLU_177471_0_0_2; -.
DR OMA; ISTSEDY; -.
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-KW.
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 InterPro; IPR021985; RNA_pol_Rpo13.
DR Pfam; PF12136; RNA_pol_Rpo13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..105
FT /note="DNA-directed RNA polymerase subunit Rpo13"
FT /id="PRO_0000453721"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 38..57
FT /evidence="ECO:0007829|PDB:7OQY"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:7OQY"
SQ SEQUENCE 105 AA; 12308 MW; EEA9700018878322 CRC64;
MSEDDSKKEP EPEETEAEIK HEEISREEDD EGGEFSTVTI SDIEMLLKDT EIWDKLLRNE
LSIEEAKKMF DDVARSYSKA DKKKRRVEKK PKKGKVTKKS DEEEE
