RPOC_VESOH
ID RPOC_VESOH Reviewed; 1393 AA.
AC A5CW24;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=COSY_0735;
OS Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Vesicomyosocius.
OX NCBI_TaxID=412965;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA;
RX PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA Kato C., Kitagawa M., Kato I., Maruyama T.;
RT "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT clam, Calyptogena okutanii.";
RL Curr. Biol. 17:881-886(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; AP009247; BAF61847.1; -; Genomic_DNA.
DR RefSeq; WP_011930117.1; NC_009465.1.
DR AlphaFoldDB; A5CW24; -.
DR SMR; A5CW24; -.
DR STRING; 412965.COSY_0735; -.
DR PRIDE; A5CW24; -.
DR EnsemblBacteria; BAF61847; BAF61847; COSY_0735.
DR KEGG; vok:COSY_0735; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000247; 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; 1.
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..1393
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353454"
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 1393 AA; 154882 MW; E2D8903143889DBC CRC64;
MRDLLKIHKL EQKEQDFDAI RVGLASPEKI RSWSYGEVKK PETINYRTFK PEREGLFCAK
VFGPMKDFEC LCGKYKRMKF RNVVCEKCGV EVTYSKVRRE RMGHIELAAP VAHIWYLKSL
PSRLGLLMDM TLKDIERVLY FEAFLVTDPG STPLVHKQLL TEEMYFDALD EYGDDEFEAK
MGAEAIQDVL SDMKLEVEAA NLREDSLNTK SQTKLKKYNK RLKLVNSLIQ SGNKPEWMVL
KVLPILPSDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL ARLLELDAPE IIVRNEKRML
QEAVDSLIDN GRRGRAVMGN NRRPLKSISD MIKGKQGRFR QNLLGKRVDY SGRSVIVCGP
YLKLHQCGLP KKMALELFKP FIYNRLQTKG LASTIKAAKK MVESESPEVW DILERVVHQH
PVLLNRAPTL HRLGIQAFEP LLIEGKAIQL HPLVCGAFNA DFDGDQMAVH VPLSEEAQLE
ARTLMLASNN VLHLASGEPI IVPSQDVILG LYYMTREMIN QKGEGLIFVN ATEALNAYES
DSVTLHAKVK LRIQDYHKVN GKFEPSAKRI VDTTVGRAIF SRILPNGLSF NLINEAISKK
VVSNLIHVCY RTQELKQTVM FADQMMYMGF QYSTKSGISF CSNDMIIPDS KAKMIEQAEI
QVKDIQEQFS KGVVTDGERY NKVIDIWSRT SEKVAKAMMD EIGFENFTDV DGKIQKLASF
NSVYMMADSG ARGSPAQMRQ LSGMRGLMAK PDGSIIETPI TSNFREGLNN MQYFISTHGA
RKGLADTALK TANSGYLTRR LVDVGQDLVI TENDCGTDNG LIMKAVIDGG NIVQTLGTAT
LGRVTAEDVL MPDSIEIFLE KGHLVSLDDS DKINELGIES IKVRSSITCD TRYGVCSSCY
GNDMARGHKI GVGEAIGVIA AQSIGEPGTQ LTMRTFHIGG AASASTAVSS INVNTDGIAH
FENLKSITNE NNDLVVISRS SEVTIRNNKG QEVERYKIPY GAIVHVQEGG AVTAKDKISD
WDPHTHPIIS EQAGRVIFVD FVEGMTVNKN TDPLTGLTFF EMIDEAERST AAKGLKPLIK
MVEENDSEVV LSTHYLPSTV KINLDDNQVI AAGGVLAKIP KDLSKTSDIT GGLPRVADLF
EARKAKDHSI LAEATGVISF GNSTKSKDRL IITSSEGKAT EMMIHKWSQI NVFDGETIEK
GDVISDGPSN PHDILRLLGV EALANYVVRE VQNVYRLQGV NISDKHIEVI VKQMLRKVEI
LDAGDSSFVN GETAEYGRVI EMNYQLEAQG KDLINYQRLL MGITKASLAT ESFISAASFQ
ETTRVLTEAS TTGRVDTLQG LKENVIVGRL IPAGTGFKHH QVRRAQYVES ITTQTVDAQQ
ALSDQLKEAE EQT
