RPO13_SACSH
ID RPO13_SACSH Reviewed; 104 AA.
AC B8YB65;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo13 {ECO:0000303|PubMed:19419240};
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:Q4JAJ6};
GN Name=rpo13 {ECO:0000303|PubMed:19419240};
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 (3.52 ANGSTROMS)
RP OF THE RNA POLYMERASE COMPLEX, FUNCTION, 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,
RP FUNCTION, AND 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, SUBCELLULAR LOCATION, DOMAIN, DNA-BINDING, AND
RP MUTAGENESIS OF 1-MET--PHE-33 AND 81-ARG--GLY-104.
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 (Probable). A molten-globule protein, it
CC binds dsDNA in the RNAP, in vitro binds dsDNA but not ssDNA (Probable)
CC (PubMed:22848102). Its position in RNAP implies it functions in both
CC transcription initiation and elongation (Probable).
CC {ECO:0000269|PubMed:22848102, ECO:0000305|PubMed:19419240,
CC ECO:0000305|PubMed:21265742, ECO:0000305|PubMed:22848102}.
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. Rpo1N and Rpo5
CC form a cleft which docks Rpo13 (PubMed:19419240, PubMed:21265742,
CC PubMed:22848102). Forms predominantly dimers in solution, although
CC monomers and trimers can also be seen (PubMed:21265742,
CC PubMed:22848102). Found associated with RNAP but also as a homodimer
CC pool in the cytoplasm in vivo (PubMed:22848102).
CC {ECO:0000269|PubMed:19419240, ECO:0000269|PubMed:21265742,
CC ECO:0000269|PubMed:22848102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22848102}.
CC -!- DOMAIN: Forms a helix-turn-helix motif with helix 1 (residues 38-56)
CC nearly parallel to helix 2 (residues 61-82); helix 1 contacts both Rpo5
CC and Rpo1N. The C-terminal region (residues 81-104) is required for DNA-
CC binding. {ECO:0000269|PubMed:22848102}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo13 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; FJ515677; ACL36500.1; -; Genomic_DNA.
DR PDB; 2WAQ; X-ray; 3.35 A; Q=38-82.
DR PDB; 2WB1; X-ray; 3.52 A; J/Q=1-104.
DR PDB; 2Y0S; X-ray; 3.80 A; J/Q=1-104.
DR PDB; 4AYB; X-ray; 3.20 A; Q=1-104.
DR PDB; 4V8S; X-ray; 4.32 A; AJ/BQ=1-104.
DR PDBsum; 2WAQ; -.
DR PDBsum; 2WB1; -.
DR PDBsum; 2Y0S; -.
DR PDBsum; 4AYB; -.
DR PDBsum; 4V8S; -.
DR SMR; B8YB65; -.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR DisProt; DP01001; -.
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; Transcription; Transferase.
FT CHAIN 1..104
FT /note="DNA-directed RNA polymerase subunit Rpo13"
FT /id="PRO_0000453788"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..104
FT /note="Required to bind DNA"
FT /evidence="ECO:0000269|PubMed:22848102"
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 BINDING 32
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="template DNA"
FT /evidence="ECO:0000305|PubMed:22848102"
FT MUTAGEN 1..33
FT /note="Missing: Decreased stability, still binds DNA."
FT /evidence="ECO:0000269|PubMed:22848102"
FT MUTAGEN 81..104
FT /note="Missing: Protein is stable, no longer binds DNA."
FT /evidence="ECO:0000269|PubMed:22848102"
FT HELIX 38..56
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 61..81
FT /evidence="ECO:0007829|PDB:4AYB"
SQ SEQUENCE 104 AA; 12148 MW; CBDD4D7126D8497F CRC64;
MVSGMSTEEE KEGTNDEEVS EEREVEETSE EEFPKLSIQD IELLMKNTEI WDNLLNGKIS
VDEAKRLFED NYKDYEKRDS RRKAKKAASK KVKKTKKKEK SVEG
