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Database: UniProt
Entry: E8X1S8_GRATM
LinkDB: E8X1S8_GRATM
Original site: E8X1S8_GRATM 
ID   E8X1S8_GRATM            Unreviewed;      1396 AA.
AC   E8X1S8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000256|HAMAP-Rule:MF_01322};
GN   OrderedLocusNames=AciX9_0930 {ECO:0000313|EMBL:ADW67997.1};
OS   Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN   [1] {ECO:0000313|Proteomes:UP000000343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA   Haggblom M.M., Woyke T.;
RT   "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL   Submitted (JAN-2011) 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:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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:0000256|ARBA:ARBA00024550,
CC         ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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DR   EMBL; CP002480; ADW67997.1; -; Genomic_DNA.
DR   RefSeq; WP_013579321.1; NC_015064.1.
DR   STRING; 1198114.AciX9_0930; -.
DR   PaxDb; 1198114-AciX9_0930; -.
DR   KEGG; acm:AciX9_0930; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_0; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000000343; 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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd02655; RNAP_beta'_C; 1.
DR   CDD; cd01609; RNAP_beta'_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.1790.20; -; 1.
DR   Gene3D; 1.10.40.90; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 3.
DR   Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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   NCBIfam; TIGR02386; rpoC_TIGR; 1.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_01322};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01322};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01322};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01322}; Reference proteome {ECO:0000313|Proteomes:UP000000343};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01322};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01322}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT   DOMAIN          236..515
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   COILED          1359..1394
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         461
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         463
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         465
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         815
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         888
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         895
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         898
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1396 AA;  156267 MW;  1F4D4541577DA85A CRC64;
     MFRSSPFELT GPIADFDAIK IQLASPEKIR SWSHGEVTKP ETINYRTFKP ERDGLFCARI
     FGPITDWECL CGKYKRMKHR GVICDKCGVE VTLSKVRRER LGHIELASPC SHVWFFKGLP
     SRIGHLLDIS LRELEAVLYF ESYVVVDPGD APVKEREVIK DEARYRELDT QYRVSGFKAM
     MGAEAIKELL KRVEIIELSI ELRERMKTET SLQKKLKYSK RLKIVEAFRK SDNLPQWMIL
     DVIPVIPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KKLMDLHAPE VIVRNEKRML
     QEAVDALFDN GRRGRVLRGA NNRPLKSLSD TLKGKQGRFR QNLLGKRVDY SGRSVIVVGP
     ELKLHQCGLP KKMALELFKP FIYHRLEQTG HCTTIKQAKE MVEMQEPIVW DILEEVIKDH
     PVLLNRAPTL HRLGIQAFEP VLVEGKAIKI HPLVCTAFNA DFDGDQMAVH IPLSPEAQIE
     ASVLMLASHN ILSPASGQPI TVPTQDLVLG LYYLTKAKVN AKGEGRVFAN IEEVFMALEA
     KQVETLTPIR LRYTGMVLDM TTAYDDQDLT HTEPVEYKNQ FISTTVGRAI LNDALPEDMP
     FVNGLLKKKG IGQLINYCYL NLGLEVTVKT LDRVKDLGFT YATRSGLSVG LDDMVIPDSK
     YTVVAEAEKQ VINVQQQYLD GAITNGERNN KVIQLWSTVT ERVADEMFNN MKQADKDGAM
     NPIYIMADSG ARGSKQQIRQ LSGMRGLMAK PSGEIIETPI TANFREGLTV LQYFISTHGA
     RKGLADTALK TADSGYLTRR LVDVAQDVII SHNDCGTVEG IYVTPIIEAG ETIEPLRDRI
     IGRVSLEKLK DFEGKVIVDI NEEIDEDKAS AVQAAGIEKV KIRSVLTCES KRGCCILCYG
     RNLGSGKMVE MGEAVGVIAA QSIGEPGTQL TMRTFHIGGT ASRVSDASHL EAKNAGSVRF
     INLVTVRSKE GHLVAFNRNG SIAIIDEKGR EKERYAIVYG AKLRVEDGVQ VKQGDYLGEW
     DPYTFSLLTE IAGTVQFKDL QEGVTLNEEV DEVTGLSRLV VADSPDEKRQ PTIIIKSAQG
     NKRYLMPSRA HLMIQDGDEV HPGDILAKIP RETTRTKDIT GGLPRVVELF EARKPRDPAI
     ISKIDGVVRF GDVSKGQRKV YVTADNGQEE EYSVPRGVYV NVQEGERLRA GDPLIDGPRS
     PHDVLEVLGE RAVQMYLVNE IQEVYRLQGV TISDKHIETI VRQMLRWVKI EEVGDTNFLV
     DQQTDRFRFN EENQRVLMTG GRPAIGRSLL LGITKASLST DSFISAASFQ ETTRVLTEAS
     INGSIDTLRG LKENVIVGRL IPAGTGMEYY RNVQLSPELE EAAAQVQQEV TAAIEAEERE
     LEQMRMEGEQ EEMAAE
//
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