RPOC_PARDP
ID RPOC_PARDP Reviewed; 1402 AA.
AC A1B017;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Pden_0749;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) 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; CP000489; ABL68861.1; -; Genomic_DNA.
DR RefSeq; WP_011747094.1; NC_008686.1.
DR AlphaFoldDB; A1B017; -.
DR SMR; A1B017; -.
DR STRING; 318586.Pden_0749; -.
DR PRIDE; A1B017; -.
DR EnsemblBacteria; ABL68861; ABL68861; Pden_0749.
DR KEGG; pde:Pden_0749; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000000361; Chromosome 1.
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; 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..1402
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353400"
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 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1402 AA; 155462 MW; 15F320367269FAA6 CRC64;
MNQELATNPL NPLAAPRQFD EIKISLASPE EILAWSYGEV KKPETINYRT FKPERDGLFC
ARIFGPIKDY ECLCGKYKRM KYRGLVCEKC GVEVTLQKVR RERMGHIELA APVAHIWFLK
SLPSRIGLML DMTLRDLERI LYFENYVVIE PGLTDLSYGQ LLTEEEFLDA QDQYGADAFT
ANIGAEAIRE MLANIDLAAT AEQLREELKE ATGELKPKKI IKRLKIVESF LESGNRPEWM
VLTVIPVIPP ELRPLVPLDG GRFATSDLND LYRRVINRNN RLKRLIELRA PDIIVRNEKR
MLQESVDALF DNGRRGRVIT GNNKRPLKSL SDMLKGKQGR FRQNLLGKRV DFSGRSVIVT
GPELKLHQCG LPKKMALELF KPFIYSRLEA KGLSSTVKQA KKLVEKERPE VWDILDEVIR
EHPVLLNRAP TLHRLGIQAF EPILIEGKAI QLHPLVCSAF NADFDGDQMA VHVPLSLEAQ
LEARVLMMST NNVLSPANGA PIIVPSQDMV LGLYYTTMER EGMKGEGMAF TSLEEVEHAL
ASGAVHLHAR ITARLPQIDE NGNEVITRFE TTPGRLRLGA LLPKNAKAPF ELVNRLLRKK
DIQNVIDTVY RYCGQKESVI FCDQIMGLGF REAFRAGISF GKDDMVVPPT KWDLVEETQD
QVKQFEQQYL DGLITQGEKY NKVVDAWSKC NDRVTDAMMK TISATKKDEK GAELEPNSVY
MMAHSGARGS VSQMKQLGGM RGLMAKPNGE IIETPIISNF KEGLTVLEYF NSTHGARKGL
SDTALKTANS GYLTRRLVDV AQDCIIREHD CGTDHAITAS AAVNDGEVVS PLSERVLGRV
AAEDVLVPGE DVVIVRKNEL IDERKADEIE AAGVQNVRIR SALTCESDDG VCALCYGRDL
ARGTLVNIGE AVGIIAAQSI GEPGTQLTMR TFHIGGIAQG GQQSFIAAAQ EGTVAFENES
TLENANGELI VMSRNMQLHI KSATGDTLAS HKLFYGSKLF VREGDAVARG QKMFEWDPYT
LPIIAEKAGV AKYVDLISGI SVRDETDDAT GMTQKIVTDW RSAPKGNELK PEIIIVDQDG
EPVRNEQGNP VTYPMSVEAI LSVEDGQEIK AGDVVARIPR EGAKTKDITG GLPRVAELFE
ARRPKDHAII AEIDGYVRFG KDYKNKRRIA IEPADDTLEP VEYMVPKGKH IPVQEGDFVQ
KGDYIMDGNP APHDILRIMG IEALADYLID EVQDVYRLQG VKINDKHIEV IVRQMLQKIE
ILDSGDTTLL KGEHVDRDEF EEENAKIEAK GGRQATGEPV LLGITKASLQ TRSFISAASF
QETTRVLTEA AVQGKRDKLV GLKENVIVGR LIPAGTGGAT ARVRRIATDR DQEVIEARRA
EAEAAAALIA PEDTPAEVGG ED
