RPOC_AYWBP
ID RPOC_AYWBP Reviewed; 1353 AA.
AC Q2NJ16;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=AYWB_460;
OS Aster yellows witches'-broom phytoplasma (strain AYWB).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=322098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYWB;
RX PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT "Living with genome instability: the adaptation of phytoplasmas to diverse
RT environments of their insect and plant hosts.";
RL J. Bacteriol. 188:3682-3696(2006).
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; CP000061; ABC65577.1; -; Genomic_DNA.
DR RefSeq; WP_011412741.1; NC_007716.1.
DR AlphaFoldDB; Q2NJ16; -.
DR SMR; Q2NJ16; -.
DR STRING; 322098.AYWB_460; -.
DR EnsemblBacteria; ABC65577; ABC65577; AYWB_460.
DR KEGG; ayw:AYWB_460; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR PhylomeDB; Q2NJ16; -.
DR Proteomes; UP000001934; 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..1353
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240796"
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; 153982 MW; F2FB0B2CDB20281B CRC64;
MSDNRLFTSV ETLNLSSPVL EKLKLSGINT LEDFNTFTLE ELRLLLQEAF LEVLPILKNF
ALPRNLQNLD LSEAVINILT ELGMEDFQDL LQTKMAVLTK SFETNPLAFQ KLNDLFKLYN
HFPSISSDKE YGSRDYDYFK IRLAAPEEIR QWSYGEVTSY ETINYRTYKP EISGLFCQKI
FGPVVDFQCA CSKKQVSIKS QFCNKCGVEF TETKVRRERM GHIELQTPIV HTWYLNSSPS
RLAILLNIKT KQLEEIVYYV SYVVIDPGKT EFKPKEIITE TQYSEALYEF GNTFVALTGA
EAVKKLLENL NLEKTIKVLR KSLSENSKQK RESIIKRLEI IESFHQSDNK PEWMVMDVIP
VLPPGLRPMV PLDGGRFATT EVNDLYRRIL NRNNRLKKQM LQKAPRLIIK NEKRMLQEAV
DALFDNTKTS KKNVNNVEKN RPLKSLSEML RGKQGRFRQN LLGKRVDYSG RSVIIVGPDL
EMHQCGVPRE MAIILFKPFI LKKLQETKGI DKKNANTIYE KMNEEVWNAL EEVVKEHPVL
LNRAPTLHRL GIQAFDPKLI DGKAIRLHPL VTPAFNADFD GDQMAIYVPL SLEAQAEARL
LMLVSNNILD PKNGNPVVTP SQDMVLGNYY LTIEEKKDRT INSYDSAQRT AEHQFKHRNE
GTFFADINEA KTAYQNKEIH LHTRIFIKPQ TINLSFTEEQ RQKYLMTTLG KLIFNDILPP
SFPYINEPTQ FNLDVKTPDA YFLPPGTNPK QFLKKLPTPK PFNKKFLSMI IACFFKQMKI
TETSKMLDHI KNLGFKYSTI AGITVSFADI NTYSNKQELL QEVETRNIQI ETWHKDGFLT
DAERRRLVIN EWKTIRDEIQ EGLMKEFKQD NHIFMMSESG ARGSVSNFTQ LAGMRGLMNN
PKGEIIEVPV KASFREGLKV SEFFISTHGA RKGSTDTALK TAESGYLTRR LVDVTQDIVV
IKEDCNSDRG FIVEAMMSDG KEIVSLKKRI MGRFASCDIC HPKTNTLIVA RNELIIESKA
QEIITAKIKK VPIRSILTCN CEYGICAKDY GVNLATNKLV EIGEAVGVIA AQSIGEPGTQ
LTMRTFHTGG VASASDITQG LPRIEELFEV RKPKGKALIS ELKGKIKKID KIRSQNPEIV
ITEENDPDTE HRYILEPNVD ILVSKNNIVY PGQKLTSGSV DLKELLRVAG TTEVQKYILE
EVQKVYRAQN VYISDKHIEI IIHQMFKQIL IIDEGDTHLL PGTEITINKF KKANLKMLEE
KKRLAVGRPI ILGITRSSLR SDSLLSAASF QETTKILIDA AIKGKTDHLY GLKENVIIGG
LIPAGTGILE TTLFKYPKEP ATTSELTKKT NQN
