RPO3_METST
ID RPO3_METST Reviewed; 270 AA.
AC Q2NFZ6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo3 {ECO:0000255|HAMAP-Rule:MF_00320};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00320};
DE AltName: Full=DNA-directed RNA polymerase subunit D {ECO:0000255|HAMAP-Rule:MF_00320};
GN Name=rpo3 {ECO:0000255|HAMAP-Rule:MF_00320};
GN Synonyms=rpoD {ECO:0000255|HAMAP-Rule:MF_00320};
GN OrderedLocusNames=Msp_0868;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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_00320}.
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_00320};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00320};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00320};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC Rule:MF_00320}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00320}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00320}.
CC -!- CAUTION: X-ray crystallography in other archaea shows this protein
CC binds a 3Fe-4S cluster, although a 4Fe-4S cluster has been suggested to
CC be present in this protein. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000102; ABC57257.1; -; Genomic_DNA.
DR RefSeq; WP_011406456.1; NC_007681.1.
DR AlphaFoldDB; Q2NFZ6; -.
DR SMR; Q2NFZ6; -.
DR STRING; 339860.Msp_0868; -.
DR EnsemblBacteria; ABC57257; ABC57257; Msp_0868.
DR GeneID; 41325443; -.
DR KEGG; mst:Msp_0868; -.
DR eggNOG; arCOG04241; Archaea.
DR HOGENOM; CLU_038421_3_1_2; -.
DR OMA; ECLRHPE; -.
DR OrthoDB; 72726at2157; -.
DR Proteomes; UP000001931; 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:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1.
DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1.
DR InterPro; IPR036643; RNApol_insert_sf.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE 3: Inferred from homology;
KW 3Fe-4S; Cytoplasm; DNA-directed RNA polymerase; Iron; Iron-sulfur;
KW Metal-binding; Nucleotidyltransferase; Reference proteome; Transcription;
KW Transferase.
FT CHAIN 1..270
FT /note="DNA-directed RNA polymerase subunit Rpo3"
FT /id="PRO_1000005788"
FT BINDING 206
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
FT BINDING 209
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
FT BINDING 212
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
SQ SEQUENCE 270 AA; 30742 MW; 7F4B5AA74329F09F CRC64;
MNIEIREKDD ERAVFVVEGV DDTFINTIRR ICLVEIPTLA IEDVNIYKND AKMFDEVLAH
RLGLIPIVTD LDSYVMPSEC DCESGCQHCR VSFLLKEKCE EGNDSKIVYS KDLKSDDPAV
KPVYDTIPIV RLREGEEVEL EAIAELGLGS EHAKWQATTT CGYKYYPKIE IDTEKVNDLE
EYVEECPRNV LQIEDDTLVV GNIENCSTCR TCQRLSEKDD NAIVVDFEES KYIFKIETDG
SLKPFDVLTI ACDILSEKAD NIINFVNEEE
