RPOC_POLNS
ID RPOC_POLNS Reviewed; 1420 AA.
AC B1XSP4;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Pnec_0043;
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1;
RX PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT "Polynucleobacter necessarius, a model for genome reduction in both free-
RT living and symbiotic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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; CP001010; ACB43371.1; -; Genomic_DNA.
DR RefSeq; WP_012357140.1; NC_010531.1.
DR AlphaFoldDB; B1XSP4; -.
DR SMR; B1XSP4; -.
DR STRING; 452638.Pnec_0043; -.
DR PRIDE; B1XSP4; -.
DR EnsemblBacteria; ACB43371; ACB43371; Pnec_0043.
DR KEGG; pne:Pnec_0043; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
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..1420
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353405"
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 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 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 897
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"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1420 AA; 156450 MW; 9FE4BAD8D54CB9E9 CRC64;
MKALLDLFKQ TQGDEQFDVI KIGLASPEKI RSWSFGEVRK PEAINYRTFK PERDGLFCAK
IFGPTKDYEC LCGKYKRLKF RGIICEKCGV EVTLAKVRRE RMGHIELAAP VAHIWFLKSL
PSRLGMVLDM TLRDIERVLY FEAYVVVDPG MTPEGAMKRG QIMSEDEYIA KTEEYGDGVF
TAIMGAEGIR DLLRSIDIDR EVETIRADLK ATGSDAKIKK YAKRLKVLEA FQTSGIKPDW
MIMEVLPVLP PELRPLVPLD GGRFATSDLN DLYRRVINRN NRLKRLLELR APEIIVRNEK
RMLQEAVDSL LDNGRRGKAM TGANKRPLKS LAEMIKGKSG RFRQNLLGKR VDYSGRSVIV
VGPTLKLHQC GLPKLMALEL FKPFIFNKLE TLGIATTIKA AKKEVESQTP IVWDILEEVI
REHPIMLNRA PTLHRLGIQA FEPMLIEGKA IQLHPLVCAA FNADFDGDQM AVHVPLSLEA
QMEARTLMLA SNNVLFPANG EPSIVPSQDV VLGLYYATRD KINGKGEGMV FANITEVVRA
YEAGQVELAS RVAVRITEYE IVDKKAEGDA RFAGKTKIYQ TSVGRAILSE ILPKGMSFEE
INKPLKKKEI SRLINTSFRK CGLRETVIFA DRLLQSGFRL ATNAGISVAI DDMLIPTSKE
RIITEASTKV KEYDKQFMSG LVTNQERYNN VVDIWGAAGD QVGKAMMDEL SHVDVLDRNG
KTVRQESFNS IYMMADSGAR GSAAQIRQLA GMRGLMAKPD GSIIETPITA NFREGLNVLQ
YFISTHGARK GLADTALKTA NSGYLTRRLC DVTQDLVVIE EDCGATTGVT MKALVEGGEI
IEALRDRILG RVCIGDIVHP DTQEVIVPND TLLDEDHVDQ IVALGIDEVK VRTVLSCLTR
FGLCAKCYGR DLGRGGLVNV GEAVGVIAAQ SIGEPGTQLT MRTFHIGGAA SRALVASNIE
AKSNGALKFS GTMRVVKNSR GEQIVISRSG EALIVDENGR ERERHKVPYG ATLLLKEDAA
VKAGASLATW DPLTRPIISE YAGIARFDNV EEGVTVAKQV DEITGLSTLV VIDGKRRSAA
SKGVRPVINL IDDKGNDVMI AGTDHPVNIG LQVGALITVK DGQKVEVGEV LARIPIESQK
TRDITGGLPR VAELFEARSP KDAAVLAKVT GTVSFGKETK GKQRLVITDM DGEANEFLIP
KEKQVLVHDG QVVNKGEMIV EGPADPHDIL TLKGIEELAI YIVDEVQDVY RLQGVKINDK
HIEVIVRQML RRVQVTDPGD TSFITGEQVE RSKLYDENDR VIAEGKHPAQ FDNVLLGITK
ASLSTDSFIS AASFQETTRV LTEAAIMGKT DTLRGLKENV IIGRLIPAGT GLSYRRARKV
REQFERDRAQ MIAAEEEAMA NMPVEIEAEV VALTGEADPS
