RPOC_METI4
ID RPOC_METI4 Reviewed; 1390 AA.
AC B3E164;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=Minf_0805;
OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS V4)).
OC Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum.
OX NCBI_TaxID=481448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate V4;
RX PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA Feng L., Wang L., Alam M.;
RT "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT Verrucomicrobia.";
RL Biol. Direct 3:26-26(2008).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; CP000975; ACD82860.1; -; Genomic_DNA.
DR RefSeq; WP_012463142.1; NC_010794.1.
DR AlphaFoldDB; B3E164; -.
DR SMR; B3E164; -.
DR STRING; 481448.Minf_0805; -.
DR PRIDE; B3E164; -.
DR EnsemblBacteria; ACD82860; ACD82860; Minf_0805.
DR KEGG; min:Minf_0805; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000009149; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1390
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353393"
FT REGION 1365..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 810
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1390 AA; 155876 MW; C26A262A990C6BBA CRC64;
MEAKNLTARQ VLGFQKTIGF DEVRISIASP ETIESWSKGE VRNPETINYR TFKPEKGGLF
CERIFGPTKD WECACGKYKR IKYKGVICDR CGVEVTLSRV RRERMGHIKL AVPVSHIWFL
KCMPSRLGLI MDMTAKDLER VIYYEDYLVV DPGKTPLRFK QLLSEQEYRD ALAQYGEEAF
VAKMGAEAVR DILKQIDLQA LANDLTAAME GTRSKQLKKK LAKRLKLVQG LINSETRPEW
MILEVLPVIP PDLRPLVPLE GGRFATSDLN DLYRRVINRN NRLKNLLQLK TPDVIIRNEK
RMLQEAVDAL LDNGRHGRAV TGAGNRPLKS LSDMLQGKTG RFRMNLLGKR VDYSGRSVIV
IGPELKLHQC GLPKKMALVL FEPFMIRRLR ELGHVHTVRT AKKMIEKQDP LVWDVLEQVT
AGHLVLLNRA PTLHRLSIQA FEPILIEGDA IRIHPLVCTA YNADFDGDQM AVHVPLSIEA
QLEARLLMLA PLNIFSPSSG KPITTPTQDI TLGCYYLTQP PLKIKVQEQK RKPLFSDAQE
VIFAYNDGLL QMHDLILLKN PDYGRSTVFG DKNKKVIETT PGRVIFNQIW PPELGFYNKP
AGKKQLGEII LKCYQTVGRE KTVQCLDNLK ELGFAEATKA GISIGIDDMI VPAEKTRIIS
KAYEMVNVVE RQYRSGAITD GERYNKIVDI WTQATEEISG VIYKSLENNL GRPEYNPLFL
MVDSGARGNR QQVRQLAGIR GLMAKPSGEI IERPIISNFR EGLSVLEYFI STHGARKGLA
DTALKTADAG YLTRKLHDVA QDVVITMQDC GTNKGIIVQA IYEGDEEIVK LSERIYGRVC
CDEIIDPMTG RIVVRPGELI DEKKAKEIEE AGAEKVKIRS VLTCESKWGV CASCYGLNLA
TNRMARLGES VGVIAAQSIG EPGTQLTMRT FHIGGTASQV FKQPQIRARN DGIVQYIDLR
TVKTVDNHFI VLSKSGYLAV LDPSGRELER HTVIVGSIIL IPDGEMVKKG QVFVQWDPYN
VPILTEKGGI VEFRDIIEGV TVKKELDETT KQISTIVIEH KHDLHPQILI LDENTREVIA
FYGIPAGARI EVKPGDKVVA GQRIARTPRK MVQTKDITGG LPRVAELFEA RKPKDSAEIA
KIDGIVEDGG IIRGKRRILI RDPQTGSEEE HLIPLSKHLI VYKGDVVKKG QQLTEGPIVP
QEILDVCGIQ ELQEYLLNEV QEVYRLQGVE INDKHIEIII KQMLKKVKIL DAGDTSFLWE
EQVDRLKFEE ENRIIEAKGG KPAVGIPVLL GITKASLDTD SFIAAASFQD TTRVLTEAAT
LGKVDPLKGF KENIIMGNLI PSGTGFRTYR NIRLVEVAPP EFKEEKKEQK IYGNGEEPAK
EQKWIPQAGT
