RPOC_CHLAA
ID RPOC_CHLAA Reviewed; 1503 AA.
AC A9WH11;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Caur_0873;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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; CP000909; ABY34106.1; -; Genomic_DNA.
DR RefSeq; WP_012256762.1; NC_010175.1.
DR RefSeq; YP_001634495.1; NC_010175.1.
DR AlphaFoldDB; A9WH11; -.
DR SMR; A9WH11; -.
DR STRING; 324602.Caur_0873; -.
DR EnsemblBacteria; ABY34106; ABY34106; Caur_0873.
DR KEGG; cau:Caur_0873; -.
DR PATRIC; fig|324602.8.peg.1002; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR InParanoid; A9WH11; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000002008; 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; -; 2.
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; 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 TIGRFAMs; TIGR02386; rpoC_TIGR; 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..1503
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000086394"
FT REGION 1439..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1503
FT /note="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 1503 AA; 169344 MW; B68E0FA8A8AD6E95 CRC64;
MLEINDFNAI RISLASPEDI RSWSHGEVTK PETINYRTLK PERDGLFCER IFGPTKDWEC
FCGKYKRVRY KGVVCDKCGV EVTRSKVRRE RMGHINLASP VSHIWFVKGT PSRLGLLLDI
SPRNLERVLY FASYIIVEVK EDMLQVAREM IQEEYAARRQ KIQKQAEEKR IELSTQLTQD
LGGMETAQRS TQRQIEEEYR RLRDEIASEA EQLRERLEEL SGTLADEDIL FRGVTVVEEG
EPINENTLDQ LDELVEQELE VLEERRRRDL ADAELLTDAE RERKAYEATQ EQERLQERLQ
RELDHLMREE KEKLEQLDTL KVGRIITETE YRQLRDIAPG VFRADMGAGA VRELIEKTVN
LDKLAEELQA EIQSSQGQRR KKATKRLRVV EAFRKSGNRP EWMILTVLPV IPPDLRPMVQ
LDGGRFATSD LNDLYRRVIN RNNRLKRLIE LNAPEIIVRN EKRMLQEAVD ALIDNGRRGR
AVSGKGKHRL KSLSDMLKGK QGRFRQNLLG KRVDYSGRSV IVVGPNLQLH QCGLPKKMAL
ELFKPFVMRR LVERGVAHNI KNAKRAVERV RPEVWDALEE VIKDYLVLLN RAPSLHRLSI
QAFEAKLIEG SAIQLHPLVC AAFNADFDGD QMAVHVPLSR KAQEEARTRM LSKYNLLSPA
HGEPIITPSQ DIVLGCYYLT MVRDGAKGSG KRFSSIDEAM LAYEKHLLDI QAPIWIRMTG
TLSGKSDRPV RELPLAADGT PRMLIETTIG RILLNNELQP PLRFRNRLID KKGLKEIIAD
CYQYYTNLRN LSEDQLNEVR ASHGNKHVQE LARIYGSEMT AQQADRIKAL GFRYATLGGM
TIGIEDIEVP AKKYDIVREA EQLVADVEKQ FRRGLITEEE RYQEVVRIWQ EATKQTIQAV
KENLNPFGPV AMMSTSGARG NINQISQMAG MRGLMSDPTG RIIELPIKAN FREGLSVLDY
FVSTHGVRKG LADTALRTAD AGYLTRRLVD VAQDVIITIE DCGTEEGLWL HGADDDELME
KLQVRMLGRI LAAPIYHKET GELIADRNTE IDEELATAIL ASGQESVFVR SPLSCQAEHG
LCRLCYGRNL ATGKLVEIGE AVGIIAAQSI GEPGTQLTLR TFHTGGVASA DDITQGLPRV
QEIFEARVPK GKALLAEIDG VVQIVRDEEG VRTIRIVSTD VYTDEYPLGR GFSPTINHES
EVYEGQVIAE GPGGAQIVTR LTGKAFIQGD RIIVSQEDHQ ERELVVPHNA RIRVENGERV
MAGQQLTDGS ANPQELLELQ GREAVQRYLV NEAQKVYRSQ GVNINDKHIE VIVRQMLRRV
RIEDPGDTGL LPGELIDSAE FRRLNNDIVS QGGDPATAAT MLLGITKASL NTDSFLAAAS
FQETTRVLTD AAIQGKVDYL RGLKENVVIG KLIPAGTGIE KRIERPHEDL IGEMARMLEE
SQQAEEAPAE TRRATPLPTP NGNKAPESDN DALLRARLEE LLSGDGDNDQ SDAEEEDNDL
PAF
