RPOC_ONYPE
ID RPOC_ONYPE Reviewed; 1353 AA.
AC Q6YQW2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=PAM_261;
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=262768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M;
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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 1 Zn(2+) ion per subunit; 2 are expected compared to other
CC organisms. {ECO:0000305};
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, ECO:0000305}.
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DR EMBL; AP006628; BAD04346.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YQW2; -.
DR SMR; Q6YQW2; -.
DR STRING; 262768.PAM_261; -.
DR PRIDE; Q6YQW2; -.
DR EnsemblBacteria; BAD04346; BAD04346; PAM_261.
DR KEGG; poy:PAM_261; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_0_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR BioCyc; OYEL262768:G1G26-318-MON; -.
DR Proteomes; UP000002523; 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..1353
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240813"
FT REGION 1..117
FT /note="Unknown"
FT REGION 118..1353
FT /note="DNA-directed RNA polymerase subunit beta'"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 578
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 580
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 582
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1353 AA; 153591 MW; D605F128CD5E5EBE CRC64;
MSDNRLFTSV ETLNLSSPVL EKLKLSGINT LEDFNTFTLE ELRLLLQEAF LEVLPILKNF
ALPRNLQNLD LSEAVINILT ELGMEDFQDL LQTKMAVLTK AFETNPLAFQ KLNDLFKLYN
HFPSISSDKE YGSRDYDYFK IRLAAPEEIR QWSYGEVTSY ETINYRTYKP EISGLFCQKI
FGPVVDFQCA CSKKQVSIKS QFCNKCGVEF TETKVRRERM GHIELQTPIV HTWYLNSSPS
RLAILLNIKT KQLEEIVYYV SYVVIDPGKT EFKPKEIITE TQYSEALYEF GNAFVALTGA
EAVKKLLENL NLEKTIKVLR KSLSENSKQK RESIIKRLEI IESFHQSDNK PEWMVMDVIP
VLPPGLRPMV PLDGGRFATT EVNDLYRRIL NRNNRLKKQM LQKAPRLIIK NEKRMLQEAV
DALFDNAKTS KKNVNNVEKN RPLKSLSEML RGKQGRFRQN LLGKRVDYSG RSVIIVGPDL
EMHQCGVPRE MAIILFKPFI LKKLQETKGI DKKNANTIYE KMNEEVWNAL EEVVKEHPVL
LNRAPTLHRL GIQAFDPKLI DGKAIRLHPL VTPAFNADFD GDQMAIYVPL SLEAQAEARL
LMLVSNNILD PKNGNPVVTP SQDMVLGNYY LTIEEKKDRT INSYDAAQRT AEHQYKHRNE
GAFFADINEA KTAYQNKEIH LHTRIFIKPQ AINLSFTEEQ RQKYLMTTLG KLIFNDILPP
SFPYINEPTQ FNLDVKTPDA YFLAPGTNPK QFLKKLPTPK PFNKKFLSMI IACFFKQMKI
TETSKMLDHI KNLGFKYSTI AGITVSFADI NTYSNKQELL QEVEARNIQI ETWYNDGFLT
DAERRRLVIN EWKNIRDEIQ EGLMKEFQQD NHIFMMSESG ARGSVSNFTQ LAGMRGLMNN
PKGEIIEVPV KASFREGLKV SEFFISTHGA RKGSTDTALK TAESGYLTRR LVDVTQDIVV
IKEDCNSDRG FVVEAMISDG KEIVSLKQRI MGRFASCDIC HPKTNALIIA RNELITESKA
QEIITAKIKK VPIRSILTCN CEYGICAKDY GVNLATNKLV EIGEAVGVIA AQSIGEPGTQ
LTMRTFHTGG VASASDITQG LPRIEELFEV RKPKGKALIS ELKGKIKKID KIRSQNPEIV
ITEENDPDTE HRYILEPNVD ILVSKNNSVY PGQKLTSGSV DLKELLRVAG TTEAQKYILE
EVQKVYRAQN VYISDKHIEI IIHQMFKQIL IIDEGDTQLL PGTEITINNF KKANLKMLEE
NKLLAVGRPI ILGITRSSLR SDSLLSAASF QETTKILIDA AIKGKTDHLY GLKENVIIGG
LIPAGTGILE TTLFKYPKEP ATTSELAEKT NQN
