RPOC_XANOR
ID RPOC_XANOR Reviewed; 1405 AA.
AC Q8KTH8; Q5GWS7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 112.
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=XOO3590;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=XO604;
RX PubMed=12079331; DOI=10.1016/s0022-2836(02)00420-5;
RA Nechaev S., Yuzenkova Y., Niedziela-Majka A., Heyduk T., Severinov K.;
RT "A novel bacteriophage-encoded RNA polymerase binding protein inhibits
RT transcription initiation and abolishes transcription termination by host
RT RNA polymerase.";
RL J. Mol. Biol. 320:11-22(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(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; AF491331; AAM74071.1; -; Genomic_DNA.
DR EMBL; AE013598; AAW76844.1; -; Genomic_DNA.
DR RefSeq; WP_011260033.1; NC_006834.1.
DR PDB; 2MC6; NMR; -; B=1-10.
DR PDBsum; 2MC6; -.
DR AlphaFoldDB; Q8KTH8; -.
DR SMR; Q8KTH8; -.
DR STRING; 291331.XOO3590; -.
DR EnsemblBacteria; AAW76844; AAW76844; XOO3590.
DR KEGG; xoo:XOO3590; -.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000006735; 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 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1405
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067836"
FT REGION 1375..1405
FT /note="Disordered"
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 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 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT CONFLICT 631
FT /note="A -> V (in Ref. 1; AAM74071)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="E -> D (in Ref. 1; AAM74071)"
FT /evidence="ECO:0000305"
FT CONFLICT 1277
FT /note="N -> D (in Ref. 1; AAM74071)"
FT /evidence="ECO:0000305"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:2MC6"
SQ SEQUENCE 1405 AA; 155232 MW; 16AAA34E5554208F CRC64;
MKDLLNLFNQ QRQTLDFDAI KIALASPDLI RSWSYGEVKK PETINYRTFK PERDGLFCAA
IFGPIKDYEC LCGKYKRMKH RGVVCEKCGT EVTLAKVRRE RMGHIDLASP VAHIWFLKSL
PSRIGLMLDM TLRDIERVLY FEAYVVTEPG LTPLERRQLL TEEQYLTARQ EYNDDFDAAM
GAEAVYELLR TIDLQSEMTR LREEIASTGS ETKLKRLTKR IKLIEAFLES GNRPEWMVMT
VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLR RLLELNAPDI IVRNEKRMLQ
ESVDALLDNG RRGRAITGTN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVITVGPY
LKLHQCGLPK KMALELFKPF VFAKLQRRGL ATTIKAAKKL VEREEAEVWD ILEEVIREHP
VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAFNAD FDGDQMAVHV PLSLEAQLEA
RALMMSTNNI LSPANGEPII VPSQDVVLGL YYMSRALENK KGEGMVFANT SEVKRAYDNR
VVELHAKVKV RITQVDVDAV DGKRTSGTSI VDTTVGRALL SEILPEGLPF QLANTEMTKK
NISRLINSSY RLLGLKDTVV FADKLMYTGY AYATRAGVSI GIDDMLIPDE KKGILTEAEA
EVLEIQEQYQ SGLVTAGERY NKVVDIWSRT SERIAKAMMD TIGTEKVENA KGETIDQKSM
NSLYIMADSG ARGSQAQIRQ LAGMRGLMAR PDGSIIETPI KANFREGLNV QEYFNSTHGA
RKGLADTALK TANSGYLTRR LVDVAQDVVI TEIDCGTTEG LIMTPIVEGG DVVEPLKERV
LGRVVAEDVY LPGNDEEPIV TRNTLLDEAW VAKLEDASVQ SVKVRSTISC ESSFGVCARC
YGRDLARGHQ VNIGEAVGVI AAQSIGEPGT QLTMRTFHIG GAASRAAAVD NITVKTTGSV
KFNNLKSVAH ASGSLVAVSR SGELSVLDGH GRERERYKLP YGATITAKDG DAVKAGQSVA
NWDPHNHPIV SEVAGFIRFI DFVDGVTVIE KTDELTGLAS REITDPKRRG AHAKELRPIV
RIVDGKGNDL TIPNTDLPAQ YLLPPRSIVN LQDGAAVGVG DVVAKIPQEA SKTRDITGGL
PRVADLFEAR KPKDPAILAE RSGIISFGKD TKGKQRLIIK DTDGSEHEEL IPKYRQIIVF
EGEHVTKGET VVDGEPSPQD ILRLLGVEPL AAYLVKEIQD VYRLQGVKIN DKHIEVITRQ
MLRKVEIVDQ GNSKFLNGEQ VERQRVIEEN ARLVKRNELP AKYDPVLLGI TKASLATESF
ISAASFQETT RVLTEAAVRG TRDNLRGLKE NVIVGRLIPA GTGLAYHAGR RKASGLTDSE
METLSGKPAG AEPVAALADA GADEE
