RPOC_DELAS
ID RPOC_DELAS Reviewed; 1409 AA.
AC A9BR99;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Daci_0511;
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-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; CP000884; ABX33157.1; -; Genomic_DNA.
DR RefSeq; WP_012202443.1; NC_010002.1.
DR AlphaFoldDB; A9BR99; -.
DR SMR; A9BR99; -.
DR STRING; 398578.Daci_0511; -.
DR PRIDE; A9BR99; -.
DR EnsemblBacteria; ABX33157; ABX33157; Daci_0511.
DR KEGG; dac:Daci_0511; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000000784; 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.
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..1409
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141767"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 813
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1409 AA; 154709 MW; 083DA422EE7A2E68 CRC64;
MKSLLDLFKQ FTPDEHFDAI KIGLASPEKI RSWSFGEVKK PETINYRTFK PERDGLFCAK
IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRE RMGHIDLAAP CAHIWFLKSL
PSRLGLVLDM TLRDIERVLY FEAYVVTDPG MTPLKKFSIM TEDDYEAKRT EYGDEFEAKM
GAEGIKDLLE GIDIDVETER LRGDLTGSEV KVKKNAKRLK LLEAFKKSGI KPGWMVMEVL
PVLPPDLRPL VPLDGGRFAT SDLNDLYRRV INRNSRLRRL LELKAPEIIA RNEKRMLQEA
VDSLLDNGRR GKAMTGANKR ALKSLADMIK GKSGRFRQNL LGKRVDYSGR SVITVGPYLK
LHQCGLPKLM ALELFKPFIF AQLEQRGIAT TIKAAKKEVE SGTPVVWDIL EEVIKEHPVM
LNRAPTLHRL GIQAFEPILI EGKAIQLHPL VCAAFNADFD GDQMAVHVPL SVEAQMEART
LMLASNNVLF PASGEPSIVP SQDVVLGLYH ATRERINGKG EGMIFADIGE VQRALDSDQV
ELAAKISVRL TEWTKNKDSG EFEPSTSLVE TTVGRALMSE ILPKGLPFSH MNKALKKKEI
SKLINASFRK CGLKATVVFA DKLLQNGFRL STHAGISIAI GDMLVPPQKA EIIGRAEAEV
KEIEQQYVSG LVTAGERYNK VVDIWGKAGD EVSKVMMAQL AKEKVIDRHG NEVEQESFNA
IYMMADSGAR GSAAQIRQLA GMRGLMAKPD GSIIETPITA NFREGLNVLQ YFISTHGARK
GLADTALKTA NSGYLTRRLV DVTQDLVVNE DDCGTTNGAL MRAIVEGGEV IESLRDRVLG
RTTAEDVVHP ETLAVLLPAG TLLNEDGIDE LELQGVDEIK VRTALTCETR YGLCAKCYGR
DLGRGGLINL GEAVGVIAAQ SIGEPGTQLT MRTFHIGGAA SRAAIASSVE AKSNGSISFN
STMRYVSNTK GELVVISRSG EIVISDNGRE RERHKVPYGA VLTVRPDQQV KAGLILANWD
PLTRPIITEY AGQVRFENVE EGLTVAKQVD EVTGLSTLVV IDPKRRGSAK VVRPQVKLID
ANNQEVKIPG TDHSVTIGFQ VGALIQVRDG QDVGPGEVLA RIPVEGQKTR DITGGLPRVA
ELFEARTPKD KGTLAEMTGT ISFGKETKGK VRMQITDLDG KVWEELVPKE KNILVHEGQV
VNKGESIVDG PADPQDILRL LGIEELSRYI VDEVQDVYRL QGVKINDKHI EVIVRQMLRR
VVVENTGDST YIAGEQVERS EILNTNEALQ REGKIPATYS NVLLGITKAS LSTDSFISAA
SFQETTRVLT EAAIMGKRDE LRGLKENVIV GRLIPAGTGL AYHQARKAKD AMDDAERRAI
ADAEAAELAG VMADDDTAAV SVAGDASAD
