RPOC_XYLF2
ID RPOC_XYLF2 Reviewed; 1407 AA.
AC B2IA67;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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};
GN OrderedLocusNames=XfasM23_2105;
OS Xylella fastidiosa (strain M23).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405441;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M23;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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; CP001011; ACB93503.1; -; Genomic_DNA.
DR RefSeq; WP_011098326.1; NC_010577.1.
DR AlphaFoldDB; B2IA67; -.
DR SMR; B2IA67; -.
DR EnsemblBacteria; ACB93503; ACB93503; XfasM23_2105.
DR GeneID; 58017518; -.
DR KEGG; xfn:XfasM23_2105; -.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000001698; 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..1407
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141801"
FT REGION 1384..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 814
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 1407 AA; 155883 MW; 5EBAB7EFC2C085BB CRC64;
MKDLLNLFNQ QRQTLDFDAI KIGLASPALI RSWSFGEVKK PETINYRTFK PERDGLFCAA
IFGPIKDYEC LCGKYKRMKH RGVVCEKCGT EVTLAKVRRE RMGCIELASP VAHIWFLKSL
PSRIGLMLDM TLRDIERVLY FEAYVVTEPG LTPLERRQLL TEEQYLQARQ EHADDFDASM
GAEAVYELLR MIDLQSEMAR LREEIVVTGS ETKLKRLTKR IKLIEAFIES GNRPEWMILT
VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLC RLLELSAPDI IVRNEKRMLQ
ESVDALLDNG RRGRAITGTN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS ARSVIIVGPN
LRLHQCGLPK KMALELFKPF VFAKLQRRGL ATTIKGAKKL VEREEAEVWD ILEEVISEHP
VVLNRAPTLH RQGIQAFEPV LIEGKAIQLH PLVCTAFNAD FDGDQMAVHV PLSLEAQLEA
RALMMSTNNI LSPANGEPII VPSQDVVLGL YYMSRALENK KGEGMVFANT SELKRAYDNS
VVELHAKVKV RITEIETDDQ GLRNKASSIV DTTVGRALLS EILPEGLPFV LVNTEMTKKN
ISRLINSSYR MLGLKETVVF ADKLMYTGYA YATRAGVSIC IDDMLIPIEK KEILGEAEQE
VLEIQEQYQS GLVTAGERYN KVVDIWSRTN ERIAKAMMDT IGTERVVNAD GEIVDQKSMN
SLYIMADSGA RGSPQQIRQL AAMRGLMVRP DGSIIETPIK ANFREGLSVQ EYFNSTHGAR
KGLADTALKT ANSGYLTRRL VDVTQDLCVV QLDCGTAGGL TMTPIVEGGD VVEPLKDRVL
GRVVAEDVLL PGNDDEPIVT RSTLLDEQWV AKLEEAGVQS VKVRSPITCE SPFGVCALCY
GRDLARGHLV NMGEAVGVIA AQSIGEPGTQ LTMRTFHIGG TALSAAAIDN ITVKTSGSVK
FTNLKYVEHA NGTLVAVSRS GEISVLDTHG RERERYKLPY GATINVKDMA EVKSGQILAN
WDPHNHPIVS EVAGFVRFID FVDGVTVIEK TDDLTGLSSR EIADLKRRGS QGKDLRPLVR
IVDKKGNDLT IPGTDLSAQY LLPPRSIVNL QDGAPVGIGD VVAKIPQEAS KTRDITGGLP
RVADLFEARR PKDPAILAER SGVISFGKDT KGKQRLIIKD ADGSEHEELI PKYRQIIVFE
GEHVTKGETI VDGEPSPQDI LRLLGIEPLA AYLVKEIQDV YRLQGVKIND KHIEVITRQM
LRKVEIVDQG NSKFLNGEQV ERQRVIDENA KLIARNELPA KYNPVLLGIT KASLATESFI
SAASFQETTR VLTEAAVRGT RDNLRGLKEN VIVGRLIPAG TGQTYHSQRR YSSVGLTESE
METLVGRSTS SGTEVTSPSK DAIPLGG
