RPOC_CUPNH
ID RPOC_CUPNH Reviewed; 1415 AA.
AC Q0K607;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=H16_A3496;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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; AM260479; CAJ94564.1; -; Genomic_DNA.
DR RefSeq; WP_010810462.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0K607; -.
DR SMR; Q0K607; -.
DR STRING; 381666.H16_A3496; -.
DR EnsemblBacteria; CAJ94564; CAJ94564; H16_A3496.
DR GeneID; 57645626; -.
DR KEGG; reh:H16_A3496; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008210; Chromosome 1.
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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1415
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353413"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
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 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 820
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"
FT BINDING 901
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1415 AA; 156036 MW; F9B7CB77F4473C0A CRC64;
MKALLDLFKQ VQQEEQFDAI KIGLASPEKI RSWSYGEVKK PETINYRTFK PERDGLFCAK
IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTLAKVRRE RMGHIELAAP TAHIWFLKSL
PSRLGMVLDM TLRDIERVLY FEAFVVIEPG MTPLKKSQIM SEDDYLAKCD EYGEGEFVAM
MGAEGIRELL RGIDIEKQIE QIRAELQATG SEAKIKKFAK RLKVLEAFQR SGIKPEWMIL
EVLPVLPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLLELKAPE IIVRNEKRML
QEAVDSLLDN GRRGKAMTGA NKRPLKSLAE MIKGKGGRFR QNLLGKRVDY SGRSVIVVGP
TLKLHQCGLP KLMALELFKP FIFHKLETMG IATTIKAAKK EVESQTPVVW DILEEVIREH
PVMLNRAPTL HRLGIQAFEP VLIEGKAIQL HPLVCAAFNA DFDGDQMAVH VPLSLEAQME
ARTLMLASNN VLFPANGDPS IVPSQDVVLG LYYTTRDKIN GRGEGMTFAD ISEVIRAYEN
KEVELASRVN VRITEYELVD KDAEGDARFA PKITLQATTV GRAILSEILP KGLPFSVLNK
PLKKKEISRL INTAFRKCGL RETVIFADKL LQSGFRLATR AGISIAIDDM LVPPQKEKII
AEASAKVKEY DKQYMSGLVT DQERYNNVVD IWGAAGDQVG KAMMEQLQHE DVVDREGKTV
KQESFNSIYM MADSGARGSA AQIRQLAGMR GLMAKPDGSI IETPITANFR EGLNVLQYFI
STHGARKGLA DTALKTANSG YLTRRLVDVT QDLVVVEDDC GTSNGVAMKA LVEGGEVIEA
LRDRILGRVT VADVVNPETQ ETAIEAGTLL DEDLVELIDN IGVDEVKVRT PLSCDTRYGL
CGKCYGRDLG RGVLVNSGEA VGVIAAQSIG EPGTQLTMRT FHIGGAASRA AVASSVEAKA
TGTVRFTATM RYVTNAKGEL IVISRSGEAL ITDDHGRERE RHKIPYGATL LVQDGQAIKA
GTQLATWDAL TRPIVSEYTG TTKFENVEEG VTVAKQMDEV TGLSTLVVID AKRRTAATKG
IRPQVKLLDA NGQEVKIPGT DHSVTIGFQV GALITVKDGQ QVHVGEVLAR IPTESQKTRD
ITGGLPRVAE LFEARSPKDA AVLAEVTGTT SFGKDTKGKQ RLVITDLDGN AHEFLIAKEK
QVLVHDGQVV NKGEMIVEGP ADPHDILRLK GIEELAHYIV DEVQDVYRLQ GVKINDKHIE
VIVRQMLRRV QIADVGDTKF IPGEQVERSE LLDENDRVIA EGKRPATYEN LLLGITKASL
STDSFISAAS FQETTRVLTE AAIMGKTDDL RGLKENVIVG RLIPAGTGLA YHRARKAREA
SERERAQAIA EEEQSLFIEP APVVQATTEG EGDNA
