ID K9YDX7_HALP7 Unreviewed; 1335 AA.
AC K9YDX7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
DE Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324};
GN OrderedLocusNames=PCC7418_2116 {ECO:0000313|EMBL:AFZ44278.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ44278.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|ARBA:ARBA00004026, ECO:0000256|HAMAP-Rule:MF_01324}.
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:0000256|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01324};
CC -!- SUBUNIT: In cyanobacteria the RNAP catalytic core is composed of 2
CC alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC factor is associated with the core the holoenzyme is formed, which can
CC initiate transcription. {ECO:0000256|ARBA:ARBA00025825,
CC ECO:0000256|HAMAP-Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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DR EMBL; CP003945; AFZ44278.1; -; Genomic_DNA.
DR STRING; 65093.PCC7418_2116; -.
DR KEGG; hao:PCC7418_2116; -.
DR PATRIC; fig|65093.3.peg.2244; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR Proteomes; UP000010481; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
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; IPR038120; Rpb1_funnel_sf.
DR NCBIfam; TIGR02388; rpoC2_cyan; 2.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01324};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01324}; Reference proteome {ECO:0000313|Proteomes:UP000010481};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01324}; Zinc {ECO:0000256|HAMAP-Rule:MF_01324}.
FT DOMAIN 21..81
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04983"
FT DOMAIN 110..188
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 191..1224
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1335 AA; 147134 MW; C96D62376F65CF96 CRC64;
MGKQTTNDEE QTRKDKGQMT KDKPQKIFWN QVVDKKQLKK LIHWAFINYG SASCSTMADE
LKNMGFRYAT QAGVSISVED LQVPPSKREM LESAENTIAD TEERYRIGKI TEVERFQKVI
DTWNVTSEAL KDEVVRNFQA TDPLNSVYMM SQSGARGNLS QVRQLVGMRG LMADPQGEII
DLPIKTNFRE GLTVTEYIIS SYGARKGLVD TALRTADSGY LTRRLVDVSQ DVIVREEDCG
TERGITLTSM TDGERTLIPL SDRLFGRTLA EDVVDPETGE VIVSGREYVD HNGKPTQEPV
KDSATGEYKT TARHIDEPLA EKIAAAVKEV KVRSPLTCEA ARSVCQCCYG WSLAHGRPVD
KGEAVGIIAA QSIGEPGTQL TMRTFHTGGV FTGDIAQQVT SPGEGTVVIP KKLRTRKVRT
RHGEEREQVE VSGEISVKLA EGDEQTIPVT PGSLLMVNNG ETVQAGQLIV EVATPKKRST
EKATKDVSSD LAGEVEFQDL IPEEKTDRQG NMTRTAQRGG LLWVLSGEVY NLLPGAEPVV
KNGSQVQPGD ILAETKLVTS KGGVVRLGTG KREIEIITAS VQLDQAQIRR SSIGSGEQYV
IHSANNQRFA LKTTPGSKVR HGEVIAELMD DTYHTETGGI VKYAGVEVEK RGKAKNGYEV
TQGGTLLWIP EECHEINKDI GLLRVEDGEY VEAGAEIVEN MYCQSSGVVE VVQKNDILRE
IVIKSGEIHL SDQEPTCGNE QLVHPGEEII PGLTADELRY VQYVETPEGN AILQRPVVEY
TIPDQPDIPS QTSINESGDV QIELRASQRL FYKDGERVKS VNGLELMRTQ LVLNIEDEDT
TENKDTLPIS VDIELLEREE EEETYVLQMV ILESLAIRRE NEGDAFSGSP QTRILVEDGQ
EIPSGEVVAR TEIQCREAGE VRGIREGAEA IRRILVVREA DKTTIPITEA PQVEEGDLVV
ANHPLAGDVV APESGKVIAV RDEAIVLRNA RPYRVSNGAV LHVENGSLVQ RGDNLVLLIY
ERSKTGDIVQ GLPRIEELLE ARKPREACVL ARRSGTAQVE YKDDETVDVK IIEADGVISD
YPISTGQNML VTDGQWVDVG TPLTDGPANP HEILEVFFDY YLEEKGMYEA ALLSLQKVQQ
FLVDEVQGVY QSQGIDISDK HIEVIVRQMT SKVKVEDGGD TIRLPGELAD LREVHKDNET
MYIIGGAPVE YKPNLLGITK ASLNTDSFIS AASFQETTRV LTEAAIEGKS DWLRGLKENV
IIGRLIPAGT GFSVHEESLG RSVIEEEPNP AQNMIFQSDV PETQSNSNGG LVDDQTARNY
QLSDEEFSDV VDDED
//
