RPOC_RUTMC
ID RPOC_RUTMC Reviewed; 1395 AA.
AC A1AX74;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Rmag_0810;
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthia.
OX NCBI_TaxID=413404;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
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; CP000488; ABL02531.1; -; Genomic_DNA.
DR RefSeq; WP_011738156.1; NC_008610.1.
DR AlphaFoldDB; A1AX74; -.
DR SMR; A1AX74; -.
DR STRING; 413404.Rmag_0810; -.
DR PRIDE; A1AX74; -.
DR EnsemblBacteria; ABL02531; ABL02531; Rmag_0810.
DR KEGG; rma:Rmag_0810; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002587; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1395
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353426"
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 815
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1395 AA; 155261 MW; BE16D6FEEBDAED35 CRC64;
MRDLLKIHKL EQKEQDFDAI RVGLASPEKI RSWSYGEVKK PETINYRTFR PEREGLFCAK
IFGPMKDFEC LCSKYKRMKF RNVVCEKCGV EVTHSKVRRE RMGHIELAAP VAHIWYLKSL
PSRLGLLMDM TLKDIERVLY FEAFLVTDPG STSLVHKQLL TEEMYFDALD EYGDDEFEAK
MGAEAIQDVL SDMKLEVEAA NLRENSLNTK SQTKLKKYNK RLKLVNSLIQ SGNKPEWMVL
KVLPVLPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL ARLLELDAPE IIVRNEKRML
QEAVDSLIDN GRRGRSVMGN NRRPLKSISD MIKGKQGRFR QNLLGKRVDY SGRSVIVCGP
YLKLHQCGLP KKMALELFKP FIYNRLQVKG LASTIKVAKK MVESESPEVW DVLERVVHQH
PVLLNRAPTL HRLGIQAFEP LLIEGKAIQL HPLVCGAFNA DFDGDQMAVH VPLSEEAQLE
ARTLMLASNN VLHLASGEPI IVPSQDVILG LYYMTREMIN QKGEGLIFAN ATEALNAYES
GNVTLHAKVK LRIQDYQKID GKFESSTKRI VDTTVGRAIF SRILPNGLSF DLINEAISKK
VVSDLIHVCY RTQELKQTVV FADQMMYMGF QYSTKSGISF CSNDMIIPDS KAKMIEQAKT
QVKDIQEQFS KGVVTDGERY NKVIDIWSRT SEKVAKAMMD EIGFEDFIDA DGKTQKLASF
NSVYMMADSG ARGSSAQMRQ LSGMRGLMAK PDGSIIETPI TSNFREGLNN MQYFISTHGA
RKGLADTALK TANSGYLTRR LVDVGQDLVI TEDDCGTDNG LIMKAVIDGG NIVQTLGVVT
LGRVTAEDIL MPDSTEVFLE KGHLVSLDDS DKINELGIES IKVRSAITCD TRYGVCSSCY
GNDMARGHKI GVGEAIGVIA AQSIGEPGTQ LTMRTFHIGG AASASTTISS VNVNTDGVAH
FENLKSITNE NNNLVVISRS SEVTIRNNKG QEVERYKIPY GAIVHVQEGG KVKAKDKIVD
WDPHTHPIIS EQAGRVIFVD FVEGVTVNKN TDPLTGLTFF EMIDEAERST AAKGLKPLIK
MVEESDSEVV LSTHYLPSTV KINLDDNQVI VAGEVLAKIP KDLSKTSDIT GGLPRVADLF
EARKAKDHSI LVEATGVISF GSSTKSKDRL IITNSEGEAI EMMIHKWRQI NVFDGETIEK
GDVISDGPSN PHDILRLLGV EALANYVVRE VQNVYRLQGV NISDKHIEVI VKQMLRKVEV
LDAGDSSFVN GETTEYVRVI ETNKQLEVQG KELIIYQRLL MGITKASLAT ESFISAASFQ
ETTRVLTEAS TTGRVDTLQG LKENVIVGRL IPAGTGFKHH QKRRAQYVAS ITQTIDAQQA
LADQLNEAEE QAQEG
