RPOC_BLOPB
ID RPOC_BLOPB Reviewed; 1416 AA.
AC Q492C0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=BPEN_576;
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=291272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN;
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ41182.1; -; Genomic_DNA.
DR RefSeq; WP_011283093.1; NC_007292.1.
DR AlphaFoldDB; Q492C0; -.
DR SMR; Q492C0; -.
DR STRING; 291272.BPEN_576; -.
DR PRIDE; Q492C0; -.
DR EnsemblBacteria; AAZ41182; AAZ41182; BPEN_576.
DR KEGG; bpn:BPEN_576; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR BioCyc; CBLO291272:BPEN_RS02840-MON; -.
DR Proteomes; UP000007794; 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..1416
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225515"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
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 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 89
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 892
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"
FT BINDING 902
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1416 AA; 158292 MW; 4E68FE9EDCA0D72F CRC64;
MKDLLRFFKI QHTQIEEFNA IKIALASPDM IRSWSFGEVK KPETINYRTF KPERDGLFCA
RIFGPIKDYE CLCGKYKRLK HRGVVCEKCG VEVTQSKVRR ERMGHIELAS PTAHIWFLKS
LPSRIGLLLD MPLRDIERVL YFESYVVVES GMTSLECRQV LTEEEYLDAL EEFGDEFEAK
MGAEAIQILL RNTNLKNECE YLREILEDSH SETKRKKITK RIKLIEAFIY SENKPEWMVL
NVLPVLPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLLDLAAPE IIVRNEKRML
QEAVDALLDN GRRGRAITGS NKRPLKSLAD MIKGKQGRFR QNLLGKRVDY SGRSVITVGP
YLKLHQCGLP KKMALELFKP FIYGKLELQG FASTIKAAKK MVDREEAVVW DILDNVIREH
PVMLNRAPTL HRLGIQAFEP VLIEGKAIQL HPLVCAAYNA DFDGDQMAVH VPLTLEAQLE
ARALMMSTNN ILSPANGEPI IVPSQDVVLG LYYMTRERSN AKGEGMVLTG PKEAECLYRL
GLADLHARIK IRITEYEYDK NGEWSKKTNL VNSTIGRSIL WMIVPKGLPF ILVNQVLGKK
AISTMLNNCY RLLGMKATVI LADQIMYTGF AYAARSGASV GIDDMMIPSK KADIIDEAES
EVVEIQEQFQ TGLVTAGERY NKVIDIWAAA NERVAQAMMD NLATETVMNR NGQLENQASF
NNIFMMADSG ARGSAAQIRQ LAGMRGLMAK PDGSIIETPI TANFREGLNV LQYFISTHGA
RKGLADTALK TANSGYLTRR LVDVAQDLVI TQDDCDTFSG IVMSPVIEGG DVKEPLRERV
LGRVLAEDIL ESNADTDSKV LIVRNTLLDE YWCDVLDEHS IDTVKVRSVV TCDTDFGVCS
KCYGRDLARG QIVNKGEAIG VIAAQSIGEP GTQLTMRTFH IGGAASRSAL ESSIQIKNTG
TVCLKNIKSV INGEGKLVVI SRNTELKIID QFSRTKESYK VPYGAVITKK NEEKVIHGEI
VAYWDPHTMP VIAEVSGFIQ FIDLIDGQSI VKQTDELTGL TSIVVLDTSE RVSSAKDLRP
TLKIVDINGY DIFIPGTDVP VQYFLPGRSV VQLVDGSRII CGDILARLPH ESSGTKDITG
GLPRVADLFE ARRPKESAIL AEISGTISFG KETKGKRRLM ISPIEDGDVY EEMIPKWRHL
NVFEGEYVDR GDIISDGPES PHDILRLRGV HAVTRYIVNE VQDVYRLQGV KINDKHIEVI
VRQMLRKATV IRSGSSDFLV GEQVEYSRIK IANRKLENEG KVKISFIRNL LGITKASLAT
ESFISAASFQ ETTRVLTESS VAGKRDELRG LKENVIVGRL IPAGTGYSYH QERVHHRHFS
NKKETEKSVI TNISSQITAD EASANLTELL NATSPK
