ID   RPO13_SACS2             Reviewed;         104 AA.
AC   Q980B8;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo13 {ECO:0000305};
DE            EC=2.7.7.6 {ECO:0000250|UniProtKB:Q4JAJ6};
GN   Name=rpo13 {ECO:0000305}; OrderedLocusNames=SSO0396;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2] {ECO:0007744|PDB:3HKZ}
RP   X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=18235446; DOI=10.1038/nature06530;
RA   Hirata A., Klein B.J., Murakami K.S.;
RT   "The X-ray crystal structure of RNA polymerase from Archaea.";
RL   Nature 451:851-854(2008).
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. Probably binds dsDNA.
CC       {ECO:0000250|UniProtKB:Q4JAJ6}.
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:0000250|UniProtKB:Q4JAJ6};
CC   -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC       {ECO:0000269|PubMed:18235446, ECO:0007744|PDB:3HKZ}.
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; AE006641; AAK40725.1; -; Genomic_DNA.
DR   PIR; F90183; F90183.
DR   RefSeq; WP_009988796.1; NC_002754.1.
DR   PDB; 3HKZ; X-ray; 3.40 A; Y/Z=1-104.
DR   PDBsum; 3HKZ; -.
DR   SMR; Q980B8; -.
DR   STRING; 273057.SSO0396; -.
DR   EnsemblBacteria; AAK40725; AAK40725; SSO0396.
DR   GeneID; 44129377; -.
DR   KEGG; sso:SSO0396; -.
DR   PATRIC; fig|273057.12.peg.392; -.
DR   eggNOG; arCOG05938; Archaea.
DR   HOGENOM; CLU_177471_0_0_2; -.
DR   OMA; ISTSEDY; -.
DR   BRENDA; 2.7.7.6; 6163.
DR   EvolutionaryTrace; Q980B8; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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..104
FT                   /note="DNA-directed RNA polymerase subunit Rpo13"
FT                   /id="PRO_0000453789"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..97
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           43..53
FT                   /evidence="ECO:0007829|PDB:3HKZ"
FT   HELIX           60..72
FT                   /evidence="ECO:0007829|PDB:3HKZ"
FT   TURN            73..76
FT                   /evidence="ECO:0007829|PDB:3HKZ"
SQ   SEQUENCE   104 AA;  12176 MW;  298E559164C310EE CRC64;
     MVSGMSTDEE KEGTSDEEVN EEKEVEETSE DEFPKLSIQD IELLMRNTEI WDNLLNGKIT
     LEEAKKLFED NYKEYEKRDS RRKAKKAVSK KVKKTKKKEK SVEG