RPOC_ORITI
ID RPOC_ORITI Reviewed; 1396 AA.
AC B3CV54;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=OTT_1793;
OS Orientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=334380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ikeda;
RX PubMed=18508905; DOI=10.1093/dnares/dsn011;
RA Nakayama K., Yamashita A., Kurokawa K., Morimoto T., Ogawa M., Fukuhara M.,
RA Urakami H., Ohnishi M., Uchiyama I., Ogura Y., Ooka T., Oshima K.,
RA Tamura A., Hattori M., Hayashi T.;
RT "The whole-genome sequencing of the obligate intracellular bacterium
RT Orientia tsutsugamushi revealed massive gene amplification during reductive
RT genome evolution.";
RL DNA Res. 15:185-199(2008).
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; AP008981; BAG41251.1; -; Genomic_DNA.
DR RefSeq; WP_012462209.1; NC_010793.1.
DR AlphaFoldDB; B3CV54; -.
DR SMR; B3CV54; -.
DR EnsemblBacteria; BAG41251; BAG41251; OTT_1793.
DR GeneID; 66653657; -.
DR KEGG; ott:OTT_1793; -.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001033; 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; -; 2.
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..1396
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353399"
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 75
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 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 817
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 901
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1396 AA; 154837 MW; 137C814F4BD81175 CRC64;
MVDITNFFKK TNKADSSQAF NRVRINIASP EQIRSWSYGE VTKPETINYR TFKPEKDGLF
CAKIFGPVKD YECLCGKYKR MKYRGIVCEK CGVEVTTSKV RRERMGHIEL ASPIAHIWFV
RSLPSRISIL LDMNLKDLER VIYFEAYIVM DPGLSPLHKG DLLTEEMLQQ AQNEYGEDNF
IVGIGAEAIR TLLAELDLKS LRNALQEEVN NVINSDFKRK KILRRLKLIE DFIGSGNKPE
WMIVTVLPII PPELRPLVML DAGRFASSDL NELYRRLINR NNRLKYLKKE EDGVPGIVLR
NEQRMVQLSA DTLFDNGKRG KAVKNSNKRP FKSLSDMLKG KQGRFRQNLL GKRVDYSGRS
VIVVGPELKL HQCGLPKQMA LELFKPFVYA ELERCGIATT IKAAKRIVEL GTPDVWNALA
KVIKHHPVLL NRAPTLHCLS IQAFEPVLIE DKAIQLHPLV CTAFNADFDG DQMAVHVPLS
TEAQLEARVL MMSTNNILSP ANGRPIIVPD KDIVLGLYYL TLSIDGEVGE GRLFGSMAEI
HHALFNKVVS LHSKIKFRKY IINADGDKVM ALVNTTPGRL ILGELLPDGD SISFDVVNKV
MTKKGISAIV DMVYRYYGQK ATVVFADKLM KLGFKYACMS GISFGMDDMI VPETKSKHVN
DTLLEVQEFE RQYSEGLITS GEKYNKVIDA WSRYTDRVAN DMMKGIAAGD QTSVGLTNQE
RLNSIFMMAD SEARSSVTQI KQLIGSKGLI AKASGEIIDR PILSNFCEGL TVFECFIGIP
GTRKGLADTA VKTKVSGHLS RKLSESAHGY FVKREDCGTT NGLIITAVVE GGVIVVTLAE
QVLGRVAVSN VYCPVTKVLI LQQGEMIDEY KVELINTAGI NSIKVRSVLT CELQEGVCAK
CYGRDLSTGK LVAIGTAVGI VAAQSIGEPG TQLTMRTFHI GGAATRGVEA SSFEAIVDGR
VKIINPNFVV NSNNKSVIMS RSCEVILADN VGQEITRYKA QYGSILLVTD GQEVTKGTAL
VVWDPYAMPI VTEKSGYVMF KDMIDGVSVK DIIDESTGIV NRVIIEPKQG RGEVVLRPRI
CLLDQNKQPL TLSNGLEAEY FLPVNSILSV EEGVNVSAGD ILARIPREFA GTKDITGGLP
RVIELFEARK PKNHAVIAEI DGCVKFGKDY KSKRRLILQP NDESHEPIEY ILPKGRHVTV
NEGDVVKKGD MLIEGSPVLQ DILKVMGVEA LGLYIINEIQ AVYRLQGVKI DNKHIEVIIT
RMLQKVEITD SGDSNFVIEE KVNKRAVINT NKKLKAKGLR EAQYRPILQG ITKASLQTES
FISAASFQET TRVLTEAAIA GKVDKLEGLK ENVIVGQTIP AGTGFYINEI KKIARQRDKE
IIAARDAELQ ENNTEA
