RPOC_ARTS2
ID RPOC_ARTS2 Reviewed; 1299 AA.
AC A0JZ92;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, 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}; OrderedLocusNames=Arth_2983;
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=290399;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24;
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
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; CP000454; ABK04362.1; -; Genomic_DNA.
DR RefSeq; WP_011692815.1; NC_008541.1.
DR AlphaFoldDB; A0JZ92; -.
DR SMR; A0JZ92; -.
DR STRING; 290399.Arth_2983; -.
DR PRIDE; A0JZ92; -.
DR EnsemblBacteria; ABK04362; ABK04362; Arth_2983.
DR KEGG; art:Arth_2983; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_11; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000754; 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..1299
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308819"
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 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 877
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 954
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 961
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 964
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1299 AA; 143599 MW; CFF447A85187FA0E CRC64;
MSSESSFGLM QIGLATAEDI RGWSYGEVKK PETINYRTLK PEKDGLFCEK IFGPSRDWEC
YCGKYKRVRF KGIICERCGV EVTRAKVRRE RMGHIELAAP VTHIWYFKGV PSRLGYLLDL
APKDLEKVIY FAAYMITSVD TDSRHEELPN LQVEHDIEKK QLVDNRDSDI ATIARDLENE
LARLEGEGAK AADKKKARDS ADRQMANVRK RADADIERLE QVWDRFKNLK VADLEGDEGL
YRELRDRYGM YFEGSMGAEA IKKRLENFDM QAESDLLRDI IANGKGQRKT RALKRLKVVN
AFLTTNNSPL GMVLDAVPVI PPELRPMVQL DGGRFATSDL NDLYRRVINR NNRLKRLLDL
GAPEIIVNNE KRMLQEAVDS LFDNGRRGRP VTGPGNRPLK SLSDMLKGKQ GRFRQNLLGK
RVDYSGRSVI VVGPQLKLHQ CGLPKQMALE LFKPFVMKRL VDLNHAQNIK SAKRMVERYR
PQVWDVLEEI ITEHPVLLNR APTLHRLGIQ AFEPQLVEGK AIQLHPLVCG AFNADFDGDQ
MAVHLPLSPE AQAEARILML SSNNILKPSD GRPVTLPSQD MIIGLYHLTT KRVGSAGEGR
IFSSVSEAIM AFDLHELHLN SQVKIRLEGF VPYAGWEAPE GWEPGQTALV QTSLGQVIFN
QTLPEDYPWV EAVADKGELS RIVNDLAERY PKVVTAATLD NLKDAGFYWA TRSGVTVAIS
DIEVPAEKPV ILAGYEERAA KIQGQYDKGL IDDDERRQEL IEIWNKATNE IAQVMRDNLS
PMNTINRMVS SGARGNWMQV RQIAGIRGLV ANPKGEIIPR PIKSSYREGL SVLEYFIATH
GARKGLADTA LRTANSGYLT RRLVDVSQDV IVREEDCGTE RGLVTPIAVA DANGELVLDE
NVENSAYART LAVDVVDSKG KVLAAGGTDC GDVVIAELFA AGITEVKVRS VLTCESSVGT
CALCYGRSLA TGKTVDIGEA VGIIAAQSIG EPGTQLTMRT FHTGGAVSAS GGDDITQGLP
RIQELFEART PKGVAPIAEA AGRIAIEESE RQMRLVITPD DGSEEIAYPV LRRSRLLIED
GQHVAVGQKL INGPVDPKQV LRIMGPRAAQ KFLVDEVQGV YRSQGIGIHD KHVEVIVRQM
LRRVTVIESG ESDLLPGELA ERSRFEDANR RVVSEGKTPA SGRPELMGIT KASLATESWL
SAASFQETTR VLTQAAMEGK SDPLLGLKEN VIIGKLIPAG TGLPRYTEVT VEPTEEAKAN
LFTGPSAFSD FSYDTLGGDG APEFHAIPLD DYDLGSDFR
