ID   RPO5_SACSH              Reviewed;          84 AA.
AC   B8YB60;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo5 {ECO:0000255|HAMAP-Rule:MF_00025, ECO:0000303|PubMed:19419240};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00025};
DE   AltName: Full=DNA-directed RNA polymerase subunit H {ECO:0000255|HAMAP-Rule:MF_00025};
GN   Name=rpo5 {ECO:0000255|HAMAP-Rule:MF_00025, ECO:0000303|PubMed:19419240};
GN   Synonyms=rpoH {ECO:0000255|HAMAP-Rule:MF_00025};
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_00025}.
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_00025};
CC   -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex. Rpo1N and Rpo5
CC       form a cleft which docks Rpo13. {ECO:0000269|PubMed:19419240,
CC       ECO:0000269|PubMed:21265742, ECO:0000269|PubMed:22848102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00025,
CC       ECO:0000269|PubMed:22848102}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_00025}.
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DR   EMBL; FJ515672; ACL36495.1; -; Genomic_DNA.
DR   PDB; 2WAQ; X-ray; 3.35 A; H=1-84.
DR   PDB; 2WB1; X-ray; 3.52 A; H/Z=1-84.
DR   PDB; 2Y0S; X-ray; 3.80 A; H/Z=1-84.
DR   PDB; 4AYB; X-ray; 3.20 A; H=1-84.
DR   PDB; 4V8S; X-ray; 4.32 A; AZ/BH=1-84.
DR   PDBsum; 2WAQ; -.
DR   PDBsum; 2WB1; -.
DR   PDBsum; 2Y0S; -.
DR   PDBsum; 4AYB; -.
DR   PDBsum; 4V8S; -.
DR   SMR; B8YB60; -.
DR   GeneID; 8761973; -.
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:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.940.20; -; 1.
DR   HAMAP; MF_00025; RNApol_Rpo5_RPB5; 1.
DR   InterPro; IPR014381; Arch_Rpo5/euc_Rpb5.
DR   InterPro; IPR000783; RNA_pol_subH/Rpb5_C.
DR   InterPro; IPR020608; RNA_pol_subH/Rpb5_CS.
DR   InterPro; IPR035913; RPB5-like_sf.
DR   PANTHER; PTHR10535; PTHR10535; 1.
DR   Pfam; PF01191; RNA_pol_Rpb5_C; 1.
DR   SUPFAM; SSF55287; SSF55287; 1.
DR   PROSITE; PS01110; RNA_POL_H_23KD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Transcription; Transferase.
FT   CHAIN           1..84
FT                   /note="DNA-directed RNA polymerase subunit Rpo5"
FT                   /id="PRO_0000453920"
FT   STRAND          12..16
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   HELIX           25..35
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   STRAND          45..49
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   HELIX           50..55
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   STRAND          62..69
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:4AYB"
FT   STRAND          73..82
FT                   /evidence="ECO:0007829|PDB:4AYB"
SQ   SEQUENCE   84 AA;  9671 MW;  2B26E5F522846532 CRC64;
     MRGSSNRKID PRIHYLVPKH EVLSIDEAYK ILKELGIRPE QLPWIRASDP VARSINAKPG
     DIIRIIRKSQ LYGEVVSYRY VISG