(data stored in ACNUC30630 zone)

SWISSPROT: RPOC_TROW8

ID   RPOC_TROW8              Reviewed;        1286 AA.
AC   Q820D9;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   11-DEC-2019, entry version 86.
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=TW082;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD66767.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; BX251410; CAD66767.1; ALT_INIT; Genomic_DNA.
DR   PRIDE; Q820D9; -.
DR   EnsemblBacteria; CAD66767; CAD66767; TW082.
DR   KEGG; tws:TW082; -.
DR   HOGENOM; HOG000218386; -.
DR   KO; K03046; -.
DR   BioCyc; GCF_000196075:G1EE9-81-MONOMER; -.
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   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime.
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; IPR038120; Rpb1_funnel_sf.
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;
DR   PRODOM; Q820D9.
DR   SWISS-2DPAGE; Q820D9.
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT   CHAIN           1..1286
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067825"
FT   METAL           58
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           60
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           73
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           76
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           533
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           535
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           537
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           867
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           944
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           951
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           954
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1286 AA;  142608 MW;  E010E9EC9AF4954C CRC64;
     MSTSFKEIRV SMATTEDIRR WSYGVVKKPE TINYRTLKPE KDGLFGEQIF GPTRDWECGC
     GKYKRSRYRG VVCERCGVEV TQSSVRRERM GHIELAAPVT HIWYFKGVPS RLGYLLDIAP
     KDLDKVIYFA AYMVVSLDEE GRKEDLQDLE NELRLDIKQL RDACDASIAS AVSELERTIT
     ELQDAKTSAS RINKVRSEAE NKMANIRREY DDKIEHLERV WDSFKALKVG GLYAEDDVFR
     DVQDRYGDYF DACMGAEAIK RRLEDFDLQK TAQELGVQIV ECRGQRKVRA IKRLRVVNSF
     ITSKANPACM VLDVIPVIPP ELRPMVQLDA GRFAASDLND LYRRVINRNN RLKRLLDLGA
     PRIIVNNEKR MLQEAVDALF DNGRRGRPVS GTNNRTLKSL SDMLKGKSGR FRQNLLGKRV
     DYSGRSVIVV GPTLQLHQCG LPKLMALELF KPFIVKRLLD LALAPNIRSA RRMIERGDPA
     VWDMLDAVIK ARPVLLNRAP TLHRLGIQAF EPQLVEGKAI QLHPLVCAAF NADFDGDQMA
     VHLPLSLEAQ AEARVLMLAS NNILNPSDGR PVTLPSHDMI IGLYHLTTVK PSAKGAGRAF
     SSVAEAIMAK DRGDLSISAP VKILFSNIVL DGKTLDSAVV ETTLGRAIFN EALPDGHPYI
     NELVDKQVIS SIINNLAEVY SKVEVANTLD KIKSVGFHWA TRSGVTVAIS DVVSPPEKQE
     IISKYETQAR GVQQDFEIGL LTDLERRQAL VSIWSEATDR VAEAMRKCFP DDNTINTMVT
     SGARGNWLQV RNIAGMRGLV ANPKGETIPR PIISSYREGL SVTEYFISTH GARKGLVDTA
     LKTADSGYLT RRLVDVAQDV VVRERDCGFT RGVRMPVTFR GDDGELHKVE NAEHSVYGRT
     LAEDVKTPDD NLIAKAGEDI SGIMIDSFIA AGVESVEVRS VLTCRSKVGV CSACYGRSLA
     TGARVDIGDA VGIVAAQSIG EPGTQLTMRT FHSGGSASAV DITQGLPRVQ ELFEARTPRA
     AAPIAEADGT VSIEDGDRAR RLILKSDNNE EFSYTVLKRA QLRVKDGSRV SLGDQLVEGS
     LDPKEVLRVK GIRAVQEYLV NGVQQVYRSQ GVPIHNKHIE VIVRQMLRKV TVVDHGDTSM
     LPGELIDQSR YQELNREAQA EGRKTASARQ EVTGITKASL ATESWLSAAS FQETTRVLTQ
     AVISGRRDPL IGLKENVIIG NLIPAGTGLS VYRDVEPEPR PEAISRMYPT RRPEIENLLE
     GDSVDPEFDF SSLTQGLELP DDYPVQ
//

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