RPOC_CERS4
ID RPOC_CERS4 Reviewed; 1415 AA.
AC Q3J5S9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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};
GN OrderedLocusNames=RHOS4_02870, RSP_1712;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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; CP000143; ABA77855.1; -; Genomic_DNA.
DR RefSeq; WP_011336949.1; NZ_AKVW01000001.1.
DR RefSeq; YP_351756.1; NC_007493.2.
DR AlphaFoldDB; Q3J5S9; -.
DR SMR; Q3J5S9; -.
DR STRING; 272943.RSP_1712; -.
DR EnsemblBacteria; ABA77855; ABA77855; RSP_1712.
DR KEGG; rsp:RSP_1712; -.
DR PATRIC; fig|272943.9.peg.585; -.
DR eggNOG; COG0086; Bacteria.
DR OMA; YRNIRVE; -.
DR PhylomeDB; Q3J5S9; -.
DR Proteomes; UP000002703; 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..1415
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225571"
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 1415 AA; 157272 MW; D53180CE87BDAC01 CRC64;
MNQELSTNPF NPVAPVKTFD EIKISLASPE RILSWSYGEI KKPETINYRT FKPERDGLFC
ARIFGPIKDY ECLCGKYKRM KYRGVVCEKC GVEVTLQKVR RERMGHIELA APVAHIWFLK
SLPSRIGLML DMTLRDLERI LYFENYVVIE PGLTDLTYGQ LMTEEEFLDA QDQYGADAFT
ANIGAEAIRE MLSAIDLEQT AETLREELKE ATGELKPKKI IKRLKIVESF LESGNRPEWM
ILTVLPVIPP ELRPLVPLDG GRFATSDLND LYRRVINRNN RLKRLIELRA PDIIVRNEKR
MLQEAVDALF DNGRRGRVIT GTNKRPLKSL SDMLKGKQGR FRQNLLGKRV DFSGRSVIVT
GPELKLHQCG LPKKMALELF KPFIYSRLEA KGLSSTVKQA KKLVEKERPE VWDILDEVIR
EHPVLLNRAP TLHRLGIQAF EPILIEGKAI QLHPLVCSAF NADFDGDQMA VHVPLSLEAQ
LEARVLMMST NNVLSPANGA PIIVPSQDMV LGLYYTTMER RGMKGEGMAF SSVEEVEHAL
AAGEVHLHAT ITARIKQIDE EGNEVVKRYQ TTPGRLRLGN LLPLNAKAPF ELVNRLLRKK
DVQNVIDTVY RYCGQKESVI FCDQIMGMGF REAFKAGISF GKDDMLIPDT KWPIVNEVRD
QVKEFEQQYM DGLITQGEKY NKVVDAWSKC SDKVAGEMMA EISAVRYDDA GAEKEPNSVY
MMSHSGARGS PAQMKQLGGM RGLMAKPNGE IIETPIISNF KEGLTVLEYF NSTHGARKGL
ADTALKTANS GYLTRRLVDV AQDCIVRTHD CGTENAITAS AAVNEGEVVS PLAERVLGRV
AAEDILVPGS DEVIVARGEL IDERRADLVD QANVASVRIR SPLTCEAEEG VCAMCYGRDL
ARGTLVNIGE AVGIIAAQSI GEPGTQLTMR TFHIGGIAQG GQQSFLEASQ EGRIEFRNPN
LLENANGEQI VMGRNMQLAI IDEAGQERAT HKLTYGAKVH VKDGQTVKRA TRLFEWDPYT
LPIIAEKAGV ARFVDLVSGI SVREDTDEAT GMTQKIVSDW RSTPKGGDLK PEIIIMNPET
GDPMRNEAGN PISYPMSVEA ILSVEDGQTV RAGDVVARIP REGARTKDIT GGLPRVAELF
EARRPKDHAI IAENDGYVRF GKDYKNKRRI TIEPVDDTLN SVEYMVPKGK HIPVQEGDFV
QKGDYIMDGN PAPHDILRIL GVEALANYMI DEVQEVYRLQ GVKINDKHIE VIVRQMLQKY
EILDSGETTL LKGEHVDKAE LDEVNQKAMD HGMRPAHAEP ILLGITKASL QTRSFISAAS
FQETTRVLTE ASVQGKRDKL VGLKENVIVG RLIPAGTGGA TSRVKKIAHD RDQKVIDTRR
AEAESAAALA APTDGVIDLG SEDSGLVETV ENREE
