RPOC2_PROM3
ID RPOC2_PROM3 Reviewed; 1374 AA.
AC A2C6T1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
GN OrderedLocusNames=P9303_04391;
OS Prochlorococcus marinus (strain MIT 9303).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9303;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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_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:0000255|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; CP000554; ABM77191.1; -; Genomic_DNA.
DR AlphaFoldDB; A2C6T1; -.
DR STRING; 59922.P9303_04391; -.
DR EnsemblBacteria; ABM77191; ABM77191; P9303_04391.
DR KEGG; pmf:P9303_04391; -.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR BioCyc; PMAR59922:G1G80-407-MON; -.
DR Proteomes; UP000002274; 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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 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 PANTHER; PTHR19376; PTHR19376; 4.
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 TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..1374
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353528"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1374 AA; 149586 MW; 656F7BEA110F3F3A CRC64;
MTSTSPKSRK PSTKTTKSKS KSKSKSKAAK AAAASASPAL ARTPPQFRNR VVDKKALKQL
VAWAYKTHGT AVTASMADNL KDLGFRYATQ AAVSISVEDL KVPEAKQDLL CQAEAQITAT
EECYRLGEIT EVERHTKVID TWTETNERLV DAVKKNFNQN DPLNSVWMMA NSGARGNMSQ
VRQLVGMRGL MANPQGEIID LPIRTNFREG LTVTEYVISS YGARKGLVDT ALRTADSGYL
TRRLVDVAQD VIVREDDCGT TRGIIVKVED GGFGSRLVGR LTADQVVNVD GEILAERNTE
IDPPLSKRFE KAAITEVMVR SPLTCEANRS VCRKCYGWAL AHNELADLGE AVGIIAAQSI
GEPGTQLTMR TFHTGGVSTA ETGVVRSTVA GTVEFGPKAR VRGYRTPHGL EAQQSEVDFT
LTVKPSGKGR AQRIDITTGS LLFVSDGQEI EADVTVVQIA SVAVKKSVEK ATKDVICDLA
GQVRYEQVIQ PREVKDRQGN ITLKAQRLGR LWVLAGDVYN LPPNAEPVVQ GNVKVERGQV
LAEASQASEF GGEVRLRDSI GDSREVQIVT TSMTMKDFKL LGESTHSGEL WHLEAKEGTR
YRLNTIPGSK IGNGEVVAEL ADDRFRTQTG GLVRFAPGLA IKKARSAKNG FEVNKGGTLL
WIPQETHEIN KDISLLMIED GQWIEAGTEV VKDIFSQTAG IVTVTQKNDI LREIIVRSGS
FHLCAETKAL ERFRGDGQIV NPGETIAKGI NSEAMVFVQT EDTPEGTGLL LRPVEEYTIP
NEAHLPELTH VKQPKGPHLG IKATQRLAFK DGELIKSVEG VELLKTQLIL ETFDTTPQMT
VDVEAVRDKR AKTIERLRLV ILESILVRRD TISDSSHGST HTELQIEDGQ SVKASDVVAT
TQILCKQEGI AQLPVPQEGD PVRRLIVERD EDTITVTTKG SPLVGVGQRL VDGDSLAKDE
PSSCCGEVEE VEGKAITLRL GRPYMVSPDS VLHVRDGDLV QRGDGLALLV FERQKTGDIV
QGLPRIEELL EARRPRESAV LCKKPGTVEI KQGEDDESIT VTVIEADDAI GEYPILLGRN
VMVSNGQQVH AGELLTDGPI NPHELLDCFF EDLRGRKPLM DAAQEAIAKL QHRLVTEVQN
VYKSQGVSID DKHIEVIVRQ MTSKVRIEDA GDTTLLPGEL IELRQVEDTN QAMAITGGAP
SEFTPVLLGI TKASLNTDSF ISAASFQETT RVLTEAAIEG KSDWLRGLKE NVIIGRLIPA
GTGFSGFQEE LRAEAGPHPD ILAEDPAGYR RMQNLRPDYT VDMPAAPAAS STAVLADPSA
ADLEATRSRH GIDPAASNFA AFVRPTGENE LEEEQLPDPS ALEGLQQEGL LTEE
