ID K8GER7_9CYAN Unreviewed; 1335 AA.
AC K8GER7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 ORFNames=OsccyDRAFT_3717 {ECO:0000313|EMBL:EKQ67443.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ67443.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ67443.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ67443.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-2012) 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: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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKQ67443.1}.
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DR EMBL; AJUB01000015; EKQ67443.1; -; Genomic_DNA.
DR STRING; 864702.OsccyDRAFT_3717; -.
DR PATRIC; fig|864702.5.peg.3986; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR Proteomes; UP000001332; 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; -; 3.
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; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001332};
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 15..70
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04983"
FT DOMAIN 99..177
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 180..1195
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT REGION 760..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 80..122
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1335 AA; 146540 MW; C329C79E524B1F4B CRC64;
MEEAGSTMVE RNNQPVFRNQ VINKKELTKM ISWAFTNYGT ARTAQMADKL KDLGFKFATR
AGVSISVDDL QVPATKRKLL EAAEETIRET EERYIRGEIT EVERFQKVID TWNGTNEELK
DEVVRNFKTN NPLNSVYMMA FSGARGNISQ VRQLVGMRGL MANPQGEIID LPIKTNFREG
LTVTEYIISS YGARKGLVDT ALRTADSGYL TRRLVDVSQD VIIREVDCGT QRGIAVRSMR
DGDRVLIPLK NRLLGRVAAQ DVVHPETGEV IVPRNQSISD DLAELIGKAN VEEVVVRSPL
TCEAVRSVCQ QCYGWSLAHA KMVDIGEAVG IIAAQSIGEP GTQLTMRTFH TGGVFTGEMA
RQERASFDGV IHYPKRLRVR PFRTRHGEDA FVVDSADPSL KITLTAEDGQ QQTFSVAQGA
TLLVRDGQKI KAGQILAEVP ITGRSRKTTE KAAKDVASDI AGEVRFADLV PEEKKDRQGN
TTRIAQRGGL LWILSGEVYN LPPGAEPVVK NGDRVEAGGV LAETKLITEH GGIVRLPQEL
EGSKGGREVE IITASVLLDQ AQVRVESYQG RDHYLIETNH NQLFSLKATP GTKVTNNQVV
AELIDDSYRT QTGGIIKYSG VEVAKRGKAK QGYEVVKGGT LLWIPEEAHE VNKDISLLLV
EDGQYVEAGT EVVKDIFCQS NGVVEVTQKN DILREIVIKP GDLHMIDNPD DIITREAILV
NPGQQVMPGL VVDELKYVEY IESPEGPALL LRPVTEFSVP DEPSVPSQES SNEDSGRSIR
LRAVQRMPYK DGERVKSVEG LELMKIQLVL EIDQDAPQLA ADIELLPDET NPDILRLQLV
ILESLVIRRD IAADQTQGST LTRILVKDGD QIAPGAVVAR TEIQCKEEGE VRGIHEGAEA
IRRVLVVRSA DLITVSTQGN PPTVKVGDLL VAGSEIAAGI TLEESGFVVQ VNDSEVVLRL
ARPYRVSPGA VLHIDDGDLV QRGDNLVLLV FERTKTGDII QGLPRIEELL EARKPREACV
LAERSGTAQV VYGEDDSVEV KVIESDGNLR EYQINPGQNV IVSDGQEVSA GERLTDGPAN
PHELLEVLFK ANRETLGVHD SSLHSLREVQ MFLVNEVQSV YQSQGIDISD KHIEVVVRQM
TSKARIDDGG DTTMLPGELV ELYQVEQVNE AMSITGGAPA EYTPVLLGIT KASLNTDSFI
SAASFQETTR VLTEAAIEGK SDWLRGLKEN VIIGRLIPAG TGFNAYEEIG SPDVDLSYEA
IGVFDDDTDL TDVVLDDRTA RTYGLDSFED HPTYGLNYGM TADSKGDLYS SILEDGEEYI
SDETDDGDDD DFEDD
//
