RPOC_ROSCS
ID RPOC_ROSCS Reviewed; 1502 AA.
AC A7NJM0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Rcas_1597;
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000804; ABU57690.1; -; Genomic_DNA.
DR RefSeq; WP_012120118.1; NC_009767.1.
DR AlphaFoldDB; A7NJM0; -.
DR SMR; A7NJM0; -.
DR STRING; 383372.Rcas_1597; -.
DR PRIDE; A7NJM0; -.
DR EnsemblBacteria; ABU57690; ABU57690; Rcas_1597.
DR KEGG; rca:Rcas_1597; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000263; 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; -; 1.
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.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1502
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000086410"
FT REGION 265..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1472..1502
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:0000255|HAMAP-Rule:MF_01322"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 626
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 628
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 630
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1002
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1075
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1082
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1085
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1502 AA; 169134 MW; BBE628AC30633270 CRC64;
MLEINDFSAI RISLASPEDI LSWSHGEVTK PETINYRTLK PERDGLFCER IFGPTKDWEC
YCGKYKRVRY KGVVCDKCGV EVTRSKVRRE RMGHISLASP VSHIWFVKGT PSRLGLLLDI
SPRNLERVLY FASYIIVHVD EEVKAHRREA LQAEYREKRE RIQAEAESRQ IELSTQLTQD
LGGMESAQLS TQRRIEEEYR RLRDEISAEA ERLRTDLEEK QGEAAEEDII FRGTVLVEEG
ESITEKTLDA LDELLDQELE TLEQRKQRDL EDAEQLTGAE RERKEYEASQ ERERLQERLQ
SELDRLVREE KERLEQLDSI KLKRILNEQE YRALREIAPG AFRADMGAGA IRDLIVRTVD
LDKLAEELQN EVYTTQGQRR KKATKRLRVV EAFRKSGNRP EWMILTVLPV IPPDLRPMVQ
LDGGRFATSD LNDLYRRVIN RNNRLKRLME LNAPEIIVRN EKRMLQEAVD ALIDNGRRGR
AVSGKGKHRL KSLSDMLKGK QGRFRQNLLG KRVDYSGRSV IVVGPDLKLH QCGLPKKMAL
ELFKPFVMRR LVEKGAAHNI KSAKRIVERV RPEVWDVLEE VIKDYLVLLN RAPSLHRLSI
QAFEAKLIEG SAIQLHPLVC AAFNADFDGD QMAVHVPLSR KAQEEARMRM LSKYNLLSPA
TGDPIITPSQ DIVLGCYYLT MVRDGAKGSG KMFASIDEAL LAYDKGLVDI QAPIFVRMTG
TLHGESDRPV RILNSDENGA PRMLLETTIG RIIFNNELLE PLRFRNRLIA KKGLREIIAD
CYKYYTNLNN LTEADLDTIR TMYGDRPRDD LARYFGSEMT ASQADRIKTL GFKYATRGGM
TIGVDDIEIP PKKQEILAEA EKRVAEVERQ FRRGLITEEE RYREIVEIWQ NATKQTTEAV
KQYLNPFGPV AMMVNSAARG NINQLSQMAG MRGLMSDPTG RIIELPIKSN FREGLSVLEY
FVSTHGGRKG LADTALRTAD AGYLTRRLID VAQDNIVTID DCGTDEGLWI YRSDDREVLQ
DFEQRILGRL LAAPLVDPRT GEVLADRNAE IDEALTRRCK ELGIDAVYVR SPLACKADYG
ICRMCYGRNL ATGKLVDIGE AVGIIAAQSI GEPGTQLTLR TFHTGGVASA DDITQGLPRV
QEIFEARTPK GKAILAEIDG IVELVREDEV RKIRVVSTDL YTDDHVLPPH YEPVVADGAQ
VNEGDVLAQS NRADLDSEPI VARLAGVVRI GAGQISVINE EREVREVIAP HTARLAAGIE
NGARVVAGQH LTEGSADPQE LLALQGREAV QRYLVNEAQK VYRSQGVDIN DKHIEVIVRQ
MLRRVRIEEP GDTDYLPGEL IDSTEFVRRN AEIISQGGEP ATASTMLLGI TKASLTTDSF
LAAASFQETT RVLTEAAITG KVDYLRGLKE NVVIGKLIPA GTGIEKRRQL AEEVIGELAN
VVPTSTAVVE QERPEREADE ALRRRLRALI GSDDNGDEVG KNGEFADETP FTGDSDDRDN
EI
