ID   RPO5_METTH              Reviewed;          77 AA.
AC   O27122;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo5 {ECO:0000255|HAMAP-Rule:MF_00025};
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};
DE   AltName: Full=RPB5 {ECO:0000303|PubMed:10841538};
GN   Name=rpo5 {ECO:0000255|HAMAP-Rule:MF_00025};
GN   Synonyms=rpoH {ECO:0000255|HAMAP-Rule:MF_00025};
GN   OrderedLocusNames=MTH_1048;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=10841538; DOI=10.1073/pnas.97.12.6311;
RA   Yee A., Booth V., Dharamsi A., Engel A., Edwards A.M., Arrowsmith C.H.;
RT   "Solution structure of the RNA polymerase subunit RPB5 from
RT   Methanobacterium thermoautotrophicum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:6311-6315(2000).
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 RNA polymerase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00025}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00025}.
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; AE000666; AAB85539.1; -; Genomic_DNA.
DR   PIR; C69006; C69006.
DR   RefSeq; WP_010876674.1; NC_000916.1.
DR   PDB; 1EIK; NMR; -; A=1-77.
DR   PDBsum; 1EIK; -.
DR   AlphaFoldDB; O27122; -.
DR   BMRB; O27122; -.
DR   SMR; O27122; -.
DR   STRING; 187420.MTH_1048; -.
DR   DNASU; 1471456; -.
DR   EnsemblBacteria; AAB85539; AAB85539; MTH_1048.
DR   GeneID; 1471456; -.
DR   KEGG; mth:MTH_1048; -.
DR   HOGENOM; CLU_058320_4_0_2; -.
DR   OMA; PKIYHDD; -.
DR   EvolutionaryTrace; O27122; -.
DR   Proteomes; UP000005223; 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: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; Reference proteome; Transcription; Transferase.
FT   CHAIN           1..77
FT                   /note="DNA-directed RNA polymerase subunit Rpo5"
FT                   /id="PRO_0000146096"
FT   STRAND          7..10
FT                   /evidence="ECO:0007829|PDB:1EIK"
FT   STRAND          13..17
FT                   /evidence="ECO:0007829|PDB:1EIK"
FT   HELIX           19..28
FT                   /evidence="ECO:0007829|PDB:1EIK"
FT   TURN            33..35
FT                   /evidence="ECO:0007829|PDB:1EIK"
FT   HELIX           44..47
FT                   /evidence="ECO:0007829|PDB:1EIK"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:1EIK"
FT   STRAND          56..63
FT                   /evidence="ECO:0007829|PDB:1EIK"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:1EIK"
FT   STRAND          67..74
FT                   /evidence="ECO:0007829|PDB:1EIK"
SQ   SEQUENCE   77 AA;  8808 MW;  745435E11D2756DC CRC64;
     MKREILKHQL VPEHVILNES EAKRVLKELD AHPEQLPKIK TTDPVAKAIG AKRGDIVKII
     RKSPTAEEFV TYRLVQD