RPOC_CHLAD
ID RPOC_CHLAD Reviewed; 1500 AA.
AC B8G4U8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Cagg_2706;
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-2008) 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; CP001337; ACL25574.1; -; Genomic_DNA.
DR RefSeq; WP_015941431.1; NC_011831.1.
DR AlphaFoldDB; B8G4U8; -.
DR SMR; B8G4U8; -.
DR STRING; 326427.Cagg_2706; -.
DR PRIDE; B8G4U8; -.
DR EnsemblBacteria; ACL25574; ACL25574; Cagg_2706.
DR KEGG; cag:Cagg_2706; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002508; 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; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1500
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000165838"
FT REGION 180..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1466
FT /note="Polar 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 1500 AA; 168949 MW; 5F96F11DADA6C99B CRC64;
MLEINDFNAI RISLASPEDI RSWSHGEVTK PETINYRTLK PERDGLFCER IFGPTKDWEC
FCGKYKRVRY KGVVCDKCGV EVTRAKVRRE RMGHINLASP VSHIWFVKGT PSRLGLLLDI
SPRNLERVLY FASYIIVDVK EDMLQVAREM VQEEYAARRE KIQKQAEEKR IELSTQLTQD
LGGMETAQRS TQRQIEEDYR RQRDELVGEA ERLRERLEEM SGTLADEDII FRGVTVVEEG
ELINDNTLDQ LDELVEQELE VLEERRRRDL ADAELLTDAE RERKAYEATQ EQERLQERLQ
RELDMLVREE KEKLEQLDKL KVGLIITENE YRQLRDVAPG VFRADMGAGA IRELLERHLN
LDKLAEELQA EIQTSQGQRR KKATKRLRIV 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 MVRDGAKGTG KRFASIDEAM LAYEKGLIDI QAPIWIRMNG
SISGKSDRPV RELPPASDGT PRMVIETTIG RVLLNSELQP PLRFRNRLID KKGLKEIIAD
CYQYYTSLRN LSEAQLNEVR AAHGNKHVQE LARIYGSEMT AQQADRIKTL GFRYATLGGM
TIGIDDIEVP AKKYDIVREA EQQVAEVEKQ FRRGLITEEE RYQEVVRIWQ EATKQTIAAV
KENLNPFGPV AMMSTSGARG NINQISQMAG MRGLMSDPTG RIIELPIKAN FREGLSVLDY
FVSTHGGRKG LADTALRTAD AGYLTRRLVD VAQDVIINIE DCGTEEGLWL HSADDGELME
KLQVRMLGRI LAAPIYDKTT GELIADRNTE IDEELAEKII AAGHESVFVR SPLTCQAEHG
LCRMCYGRNL ATGKLVEIGE AVGIIAAQSI GEPGTQLTLR TFHTGGVASA DDITQGLPRV
QEIFEARVPK GKALLAEIDG VVQIIREDEG VRKIRIVSTN VYTDEYPLTR GFTPVIESES
DVYEGQVIAE GPGGEQIIAR LSGKAFIQSD RIIISQEDHE ERELVVPHNA RIRVENGDRV
MAGQQLTDGS ANPQELLELQ GREAVQRYLV NEAQKVYRSQ GVNINDKHIE VIARQMLRRV
RIEEPGDTGL LPGELIDSAE FRRLNNDIVS QGGDPATAAT VLLGITKASL NTDSFLSAAS
FQETTRVLTD AAIQGKVDYL RGLKENVVIG KLIPAGTGIE KRLERQHEDL ISEMARMLEE
VQQAEKSAEP TTTALPTTNG HQAPQSDTDA LLRARLEELL SGGNDHDDEE DSDHPDLSSL
