ID E1II04_9CHLR Unreviewed; 1510 AA.
AC E1II04;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ORFNames=OSCT_2955 {ECO:0000313|EMBL:EFO79122.1};
OS Oscillochloris trichoides DG-6.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Oscillochloridaceae; Oscillochloris.
OX NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO79122.1, ECO:0000313|Proteomes:UP000054010};
RN [1] {ECO:0000313|EMBL:EFO79122.1, ECO:0000313|Proteomes:UP000054010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG-6 {ECO:0000313|EMBL:EFO79122.1,
RC ECO:0000313|Proteomes:UP000054010};
RX PubMed=21037015; DOI=10.1128/JB.00931-10;
RA Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V.,
RA Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., Baslerov R.V.,
RA Panteleeva A.N., Kolganova T.V., Ravin N.V., Skryabin K.G.;
RT "Draft genome sequence of the anoxygenic filamentous phototrophic bacterium
RT Oscillochloris trichoides subsp. DG-6.";
RL J. Bacteriol. 193:321-322(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFO79122.1}.
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DR EMBL; ADVR01000122; EFO79122.1; -; Genomic_DNA.
DR STRING; 765420.OSCT_2955; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR Proteomes; UP000054010; Unassembled WGS sequence.
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; -; 2.
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 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; 2.
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 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:UP000054010};
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 404..683
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT COILED 151..230
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 279..319
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 65
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 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 629
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 631
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 633
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1007
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1080
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1087
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1090
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1510 AA; 169612 MW; 0744C8587653146B CRC64;
MNPMLEINDF NAIRISLASP EDIRGWSHGE VTKPETINYR TLKPERDGLF CERIFGPTKD
WECYCGKYKR VRYKGVVCDK CGVEVTRAKV RRDRMGHITL ASPVSHIWFV KGTPSRLGLL
LDISPRNLER VLYFASYVIV EVKEDLRVVA REMLQEDYAK KRENIQRQAE DKRIELSTQL
TQDLGGMENA QVSTQRRIEE DYRRLREEIA NEAERLRERL EEMTNLVTDE DISFRNTTLV
EEGEVISERT LDQLDEMLDQ ELDTLDARRT RDMSDAELLT DAERERKAAE ATQEQEKLQE
RLQRELDTLV REEKEKLDQL DGLKPCRILS EMEYRQLRDL APGVFRADMG AGAVRELIVR
QVDLDKLAED LSAEVQTTQG QRRKKATKRL RVVESFRKSG NKPEWMIMTV LPVIPPDLRP
MVQLDGGRFA TSDLNDLYRR VINRNNRLKR LMELNAPEII VRNEKRMLQE AVDALIDNGR
RGRAVSGKGK HRLKSLSDML KGKQGRFRQN LLGKRVDYSG RSVIVVGPNL QLHQCGLPKK
MALELFKPFV MRRLVEKGFA HNIKSAKRIV ERVRPEVWDV LEEVIKDYLV LLNRAPSLHR
LSIQAFEAKL IEGSAIQLHP LVCAAFNADF DGDQMAVHVP LSRKAQEEAH TRMLSKYNLL
SPAHGDPIIT PSQDIVLGCY YISQVRDGAL GSGKKFATID EAMLAYDKGL VAIQAPIWIR
MDGMPQGKND RAENVRILKP ADDGTPRMLI ETTIGRVLLN NELLPPLRYR NRVVDKKGLR
EIIADCYQYY TNLKNVSHAD LAELRAMWPH KTDIELVRIY GSEKTAQQAD KIKALGFKNA
TYGGMTIGIN DIEVPQAKYE IVGNAEAQVF DVEKQFRRGL ITEEERYQEV VRIWQEATKL
TIVAVKENMN QFGPVAMMST SGARGNINQI SQMSGMRGLM SDPTGRIIEQ PIKANFREGL
SVLDYFVSTH GGRKGLADTA LRTAEAGYLT RRLVDVAQDV IVTIEDCGTE DGVWLHAADD
DELMERLAVR MVGRFLAAPI YDKQTGELIA DRDVEIDDDI ASKIDAHKIE SVYVRSTLTC
QSEHGICRLC YGRSLATGKL VDIGEACGIV AAQSIGEPGT QLTLRTFHTG GVASADDITQ
GLPRVQEIFE ARVPKGKSLL AEIDGVAQVV KDDDGVRTIK IIASEVYTDE YVLPKDFIAL
VDNESDVAEG QVIAESNNAD NPQPPIIARL SGRAYIYGNR IVVSQEDREE RELVVPHTAR
IRVENGARVV AGQQLTDGSA NPQELLDLQG REAVQRYLVN EAQKVYRSQG VNINDKHIEV
IVRQMLRRVR IEEPGDTGLL PGELIEAAEF RRLNNDIVSQ GGEPATAATV LLGITKASLN
TDSFLSAASF QETTRVLTDA AITGKVDYLR GLKENVVIGK LIPAGTGIEK RTERGRDELV
DEMARMMESG AAAAEQQPNN VERAESLLGI NETAAEESES DRKLRARIEE ILGSGAADDD
LGSEDDLATE
//
