RPOC_THEYD
ID RPOC_THEYD Reviewed; 1371 AA.
AC B5YFV7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-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}; OrderedLocusNames=THEYE_A1346;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001147; ACI21535.1; -; Genomic_DNA.
DR RefSeq; WP_012546248.1; NC_011296.1.
DR RefSeq; YP_002249155.1; NC_011296.1.
DR AlphaFoldDB; B5YFV7; -.
DR SMR; B5YFV7; -.
DR STRING; 289376.THEYE_A1346; -.
DR PRIDE; B5YFV7; -.
DR EnsemblBacteria; ACI21535; ACI21535; THEYE_A1346.
DR KEGG; tye:THEYE_A1346; -.
DR PATRIC; fig|289376.4.peg.1312; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR InParanoid; B5YFV7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000718; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1371
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141797"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
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 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 803
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 877
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1371 AA; 153475 MW; 6154DD59AEE0599D CRC64;
MTEDIYSLFQ KPKNPRDFDA IRIKLASPEK IREWSYGEVK KPETINYRTF KPEPEGLFCA
KIFGPIKDWE CLCGKYKRMK HKGVICDKCG VEVIQSKVRR ERMGHIELAA PVAHIWFVRG
VPSKMGLLLD LSVRQLERVI YYEDYIVIDP GDTPLKEKDI LTEDEYKKCI SQYGNKFKAG
MGAEAVRELL KKIDLDIVAQ ELKEKIEAAT STGIKRKLTK RLKVIEAFKN SGNRPEWMIL
DIVPVLPPEL RPLVPLDGGR FASSDLNDLY RRVINRNNRL KRLMELKAPS VIIRNEKRML
QESVDTLFDN TKRSKALKAG TRRPLKSLSD MIKGKQGRFR QNLLGKRVDY SGRSVIVVGP
ELDMHQCGLP KSMALELFKP FVFNKLEEKG YATTIKQAKR LVEQERSEVW DALEEVIQEH
PVLLNRAPTL HRLGIQAFDP VLVEGKAIKL HPLVCTAFNA DFDGDQMAVH VPLSYEAQVE
ARVLMMSVGN LLSPANGKPI VVPTQDMVLG IYYLTKEKHD AKGAGKVFSD PEEVILAYQC
KAVEKHAPIK VKLNGEFVNT TVGRILFREI VPEGVPFQMI NKELTKKELG KLIEYIHYNF
GKRDTVLFLN KLEKLGFEVA TQSGISICID DMHIPSKKTE LIKEAEAQVM EVQRQYAEGL
ITQGERYNKV IDIWANVTER VADEMMKELG AERGKEFTPE ELAERRSFNS IFMMADSGAR
GSIAQIRQLA GMRGLMAKPS GEIIETPITA NFREGLTPLQ YFISTHGARK GLADTALKTA
NAGYLTRRLV DVAQDIFLIE HDCGTKDGIY ITALIEGGEI VMPLEERIYG RTLAEDIKDP
LTGEIIAKRD TVIDQALAKK IVDSGIDRLK IRSVLTCRTK FGVCSKCYGM DLARSEPVEI
GEAIGVIAAQ SIGEPGTQLT MRTFHIGGAA TKIVEQAVLE AKGSGTVRFK NIHYVERKDG
SLVVLNRNAM IVITDSSGRE REKYNLVYGA KIIVKEGQIV ESGQRLAEWD AYTTPIITEI
GGKIALGDMV EGVTFKEETD PTTGLSHKII IDYPATYRPR VTIKDKDGKT AKLPSGTAAR
YLLPAGAILV VDKGDIVEPG DILAKIPRET IKTKDITGGL PRVAELFEAR RPREAAIVSE
IDGIVEFKGS QKGSRVIVVR GADETREYLI PKGKHVIVHD GDWVKAGEPL IDGSINPHSI
LEILGPTELQ RYLVDEIQKV YRLQGVSIHD KHIEVIVRQM MKKVRIEDPG DTSFLIGDEV
DRFIFIEENE KVIARGGRPA QARPLLLGIT KAALSTESWV SAASFQETTR VLTDAAIEAR
IDELRGLKEN VIMGRIIPAG TGSPVYKDTL IKGEFYSMQI EHFSEESIEE N
