RPOC_ROSS1
ID RPOC_ROSS1 Reviewed; 1504 AA.
AC A5USR6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=RoseRS_1264;
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-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}.
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DR EMBL; CP000686; ABQ89669.1; -; Genomic_DNA.
DR RefSeq; WP_011956021.1; NC_009523.1.
DR AlphaFoldDB; A5USR6; -.
DR SMR; A5USR6; -.
DR STRING; 357808.RoseRS_1264; -.
DR PRIDE; A5USR6; -.
DR EnsemblBacteria; ABQ89669; ABQ89669; RoseRS_1264.
DR KEGG; rrs:RoseRS_1264; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000006554; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1504
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000086411"
FT REGION 265..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1487
FT /note="Basic and acidic residues"
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 1504 AA; 169331 MW; F29B6580F639D851 CRC64;
MLEINDFSAI RISLASPEDI LSWSHGEVTK PETINYRTLK PERDGLFCER IFGPTKDWEC
YCGKYKRVRY KGVVCDKCGV EVTRSKVRRE RMGHISLASP VSHIWFVKGT PSRLGLLLDI
SPRNLERVLY FASYMIVHVD EELKAQAREA LQAEYREKRE RIQQEAESKQ IELSTQLTQD
LGGMESAQIT TQRRIEEEYR RLRDEISAEA ERLRSDLEEK QGEAAEEDIL FRGTVLIEEG
EIITEKTLDA LDELLDQELE TLEQRKQRDL EDAEQLTGAE RERKEYEASQ ERERLQERLQ
SELDRLVREE KERLEQIDSI KLKRILSEQE YRALREIAPG VFRADMGAGA VRDMIVRTID
LDKLAEELQN EVYTTQGQRR KKATKRLRVV EAFRKSGNRP EWMILTVLPV IPPDLRPMVQ
LDGGRFATSD LNDLYRRVIN RNNRLKRLME LNAPEIIVRN EKRMLQEAVD ALIDNGRRGR
AVSGKGKHRL KSLSDMLKGK QGRFRQNLLG KRVDYSGRSV IVVGPDLKLH QCGLPKKMAL
ELFKPFVMRR LVEKGFAHNI KSAKRIVERV RPEVWDVLEE VIKDYLVLLN RAPSLHRLSI
QAFEAKLIEG SAIQLHPLVC AAFNADFDGD QMAVHVPLSR KAQEEARMRM LSKYNLLSPA
TGDPIITPSQ DIVLGCYYLT MVKDGAKGSG KMFASIDEAL LAYDKGLIDI QAPIFVRMTG
TVYGESDRPV RMLSPDENGA PRMLLETTIG RIIFNNELLE PLRFRNRLIA KKGLREIIAD
CYKYYTNLNN LTEADLDTIR AMYGDRPRDD LARYFGSEMT ASQADRIKTL GFRYATRGGM
TIGVDDIEIP PKKQDILAEA EKRVTEVERQ FRRGLITEEE RYREIVEIWQ NATKQTTEAV
KQHLNPFGPV AMMVNSAARG NINQLSQMAG MRGLMSDPTG RIIELPIKSN FREGLSVLEY
FVSTHGGRKG LADTALRTAD AGYLTRRLID VAQDNIVTID DCGTDEGLWI YRADDREVLQ
DFEQRILGRL LAAPLVDPRT GEILANRNDE IDEALVRKCK ELAIDAVYVR SPLACKADYG
ICRMCYGRNL ATGKLVDIGE AVGIIAAQSI GEPGTQLTLR TFHTGGVASA DDITQGLPRV
QEIFEARTPK GKAILAEIDG IVELVREDEV RKIRVVATEL YTDDHELPPH YEPVVADGAQ
VNEGDVLAQS NRADLNGEPI VARIAGVVRI GAGQISVINE EREVREVVAP HTARLAPGIE
NGARVVAGQH LTEGSADPQE LLALQGREAV QRYLVNEAQK VYRSQGVDIN DKHIEVIVRQ
MLRRVRIEEP GDTDYLPGEL IDSTEFVRKN AEIISQGGEP ATASTMLLGI TKASLTTDSF
LAAASFQETT RVLTEAAITG KVDYLRGLKE NVVIGKLIPA GTGIEKRRQL AEEIIGELAN
VAPATSTAVV EQERPDREAD EALRRRLRAL IGGDGDDGER NNGDFDDQVG EDVVIPPDDD
DQEA