ID D3FET3_CONWI Unreviewed; 1355 AA.
AC D3FET3;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=Cwoe_1328 {ECO:0000313|EMBL:ADB49757.1};
OS Conexibacter woesei (strain DSM 14684 / CIP 108061 / JCM 11494 / NBRC
OS 100937 / ID131577).
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Conexibacteraceae; Conexibacter.
OX NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB49757.1, ECO:0000313|Proteomes:UP000008229};
RN [1] {ECO:0000313|EMBL:ADB49757.1, ECO:0000313|Proteomes:UP000008229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC {ECO:0000313|Proteomes:UP000008229};
RX PubMed=21304704;
RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Mavromatis K., Ivanova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Chain P.,
RA Meincke L., Sims D., Brettin T., Detter J.C., Rohde M., Goeker M.,
RA Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C., Klenk H.-P.,
RA Hugenholtz P.;
RT "Complete genome sequence of Conexibacter woesei type strain (ID131577).";
RL Stand. Genomic Sci. 2:212-219(2010).
RN [2] {ECO:0000313|Proteomes:UP000008229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC {ECO:0000313|Proteomes:UP000008229};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Conexibacter woesei DSM 14684.";
RL Submitted (JAN-2010) 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|HAMAP-Rule:MF_01322,
CC 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; CP001854; ADB49757.1; -; Genomic_DNA.
DR RefSeq; WP_012932808.1; NC_013739.1.
DR STRING; 469383.Cwoe_1328; -.
DR KEGG; cwo:Cwoe_1328; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_11; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000008229; 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; -; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 2.
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; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
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:UP000008229};
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 342..621
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1327..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 567
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 569
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 571
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 988
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 995
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 998
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1355 AA; 151097 MW; 6E8A4E6C715788F3 CRC64;
MIDINNFDAI EIGLASSKQI RSWSSGEVTK PETINYRTLK PEKDGLFCER IFGPTKDWEC
YCGKYKRVRY KGIVCERCGV EVTRSKVRRE RMGHIDLAAP VSHIWFFKGV PSRIGYLLDM
APKELEKVLY FAASIVTWID DEARERDLDS LQDEVNKVLD SYAAEKEERL LELRESLERR
VSFLESGRQS NQFNDEDEMW AEALDVNVAR LSDEEREKLL RELRRTFQAD MDDTEAYIED
AAERMRQVWD TFQSMKPKDV VNDETLFREL KDRFGSPFGF GEYFRGGMGA ESVRDLLEQV
DLDAEREELQ ELVKTAKGQK QSRSVKRLKV VSAFIQSGNR PEMMILEAVP VIPPELRPMV
QLDGGRFATS DLNDLYRRVI NRNNRLKRLL DLGAPEIIVN NEKRMLQEAV DALFDNGRRG
RPVTGPGNRP LKSLSDMLKG KQGRFRQNLL GKRVDYSGRS VIVSGPSLKL HQCGLPKLMA
LELFKPFIMA RLVERKAAQN IKAAKKMVDS MIPEVWDVLE EVIHEHPVLL NRAPTLHRLG
IQAFEPMLVE GKAIQVHPLV CHAFNADFDG DQMAVHLPLS AEAQAEARIL MLSANNILSP
AHGAPLATPT QDMILGAYYL TYGPEADELA KVDPARAAKR PHVYRTAQEA EWSYEHGVTR
LHDLAEFRPA GRQGGHILTT VGRIIYNDKI ERAIRETLGA DYDPASYEFV NRSMKKRDTT
QFVDDLVQAY GAATISQVLD AFKDLGFRYA TQAGITVSKN DVVIPPEKGE ILGKYEGEVA
EIQDQYDMGL ITEEERKDAV VDRWNAATDE VAEAMEQHFN ELNPIFMMAN SGARGSFKQI
RQLAGMRGLM ANPKGEIIER PVKANFMEGL DVIEYFTSTH GARKGLADTA LRTADSGYLT
RRLVDVAQDV IIRQEDCGAE QYVELDLYKA GGEPNDNVVG RVAALDLGPR KSVVVERGIE
MSRADFAALL EAYGEDNVKI PVRSVLKCEA PTGVCQACYG RAMATGNTAQ IGDAVGIIAA
QSIGEPGTQL TMRTFHTGGV AGADITHGLP RVVELFEARK PKGLAKIAEV GGVVEIEETD
KALTVVITDD GGDEHRHTFP RRTRLHVERG DKVEPGKQLN EGSLYPHELL AIRGRTETEL
YLVKEVQEVY KSQGVDINDK HIELIVRQML KKVRVDQKGD TDLLPGVFVD RHDYARINQV
VIDNGGEPAQ AEEIILGITK ASLNTDSFLS AASFQETTKV LTDAALEGKI DRLNGLKENV
IIGKLIPAAT GLKRYRRIEI EPAEPLPRGM DDVGLLDHDE LAAELGLTDG EALQGFGPSG
IEADLADLEE IGNGGGSHGF AEELAELDVP EDRQS
//
