ID K9TAW8_9CYAN Unreviewed; 1307 AA.
AC K9TAW8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=Ple7327_4006 {ECO:0000313|EMBL:AFY79149.1};
OS Pleurocapsa sp. PCC 7327.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC Pleurocapsa.
OX NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY79149.1, ECO:0000313|Proteomes:UP000010382};
RN [1] {ECO:0000313|EMBL:AFY79149.1, ECO:0000313|Proteomes:UP000010382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY79149.1,
RC ECO:0000313|Proteomes:UP000010382};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished genome of Pleurocapsa sp. PCC 7327.";
RL Submitted (MAY-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}.
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DR EMBL; CP003590; AFY79149.1; -; Genomic_DNA.
DR RefSeq; WP_015145447.1; NC_019689.1.
DR STRING; 118163.Ple7327_4006; -.
DR KEGG; plp:Ple7327_4006; -.
DR PATRIC; fig|118163.3.peg.4473; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR Proteomes; UP000010382; 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; 2.
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:UP000010382};
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 5..56
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04983"
FT DOMAIN 85..163
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 166..362
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1082..1174
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT REGION 1279..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1307
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1307 AA; 143024 MW; B7B9636E842E3B99 CRC64;
MVFYNHIVDK NRLKKLIAWA YRQYGSARCA QMADELKDLG FRYATKAGVS ISVDDLTIPP
TKRKLLDSAE QEIKVTEQRY ARGEITEVER FQKVIDTWNS TSESLKDEVV RNFQETDPLN
SVYMMAFSGA RGNMSQVRQL VGMRGLMADP QGEIIALPIK TNFREGLTVT EYIISSYGAR
KGLVDTALRT ADSGYLTRRL VDVAQDVIVR EIDCGTTRGI RVTAMKDGDR ILIPLADRLM
GRVLAEDVVV GGEVIAKRND SIDPELASKL GKLVDSVLVR SPLTCEAARS VCQHCYGWSL
AHGHMVDLGE AIGIIAAQSI GEPGTQLTMR TFHTGGVFTG EVARQIRAQT SGTVRYSSEL
STRKVRTRHG EDREQVEVAG DLILESDSGE SIRYSTTPGS TLFVAEGERV EAGQLLAEVA
MAKLQRSTER ATKDVASDLA GEVLFANVVP EEKTDRQGNT TRIAQRGGLV WILSGEVYNL
PPGAEPVVNN GDRVEIGTVL AETRLITNNG GVVRLTPGSR EIDIVTASVL LDKAQVKLES
TGGREQYTIY TAEGQRFLLK AAPGTKVQNH AIVAELIDDR YRTETGGMIR YAGVEVSKGT
RKQGYEVTKG GTILWIPEET HEVNKDISLL IVEDGQYVEA GTEIVKDIFC QMSGVVEVIQ
KNDILREIIV KPGDLHLDID PDVAATIELG QLVRPGTEIL PGVVVSDLRQ AEWVETTEGL
GLLLRPVVEY QVFDEPAAPS QGSINQEGGR QIELRSVQRT YFKDGERVKS VEGCQLLSTQ
LVLEISGDES DSTTTLSADI ELQEDEAEGC QRLQLVILES LVLRRETDID PHGGSIQTRV
LVEDGQQIPP GAVVARTEIQ CKEPGQVRGI RSGNEAIRRV LVVRNSDLVT LSIAEKPSVA
DGDLIVAGTQ IAPGYQASES GQVLSVRKSA DAYEVILRVA RPYRVSAGAI LHVDNGDLVQ
RGDNLVLLVF ERAKTGDIIQ GLPRIEELLE ARKPKEACVL SRKPGICQVE YLEDETVDLK
IVEDDGTVTQ YPILPGQNLM VSDGQRVGVG EPLTDGPANP HEILEVFFEY YVEEKGVYEA
ALKGLQATQS FLVDQVQSVY QSQGIDIADK HIETIVRQMT SKVRVDDGGD TTMLPGELVE
LRQIEQVNEA MAITGGAPAQ YTPVLLGITK ASLNTDSFIS AASFQETTRV LTEAAIEGKS
DWLRGLKENV IIGRLIPAGT GFNAHEDAIV NPESAEDMGY GRPLVYGVDE NSSSSRLFTN
NLEDDDNMIL DDRIARAYAG GDSNDSFEPF LDDFSPDEDE DFDGEEE
//
