RPOC2_SYNPW
ID RPOC2_SYNPW Reviewed; 1363 AA.
AC A5GNH1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=SynWH7803_2060;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) 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: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; CT971583; CAK24486.1; -; Genomic_DNA.
DR RefSeq; WP_011933951.1; NC_009481.1.
DR AlphaFoldDB; A5GNH1; -.
DR STRING; 32051.SynWH7803_2060; -.
DR EnsemblBacteria; CAK24486; CAK24486; SynWH7803_2060.
DR KEGG; syx:SynWH7803_2060; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000001566; 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; 1.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..1363
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353540"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 322
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"
SQ SEQUENCE 1363 AA; 148019 MW; FB6C8F7F844C5DFC CRC64;
MTSTPSKSRK SSKGSKAAKA AASAPETRPL AKTPPPFRNR VVDKKGLKQL VAWAYKHHGT
AATSAMADQL KDLGFRYATQ AAVSISVNDL KVPEAKQNLL GQAEELITAT EESYRLGVIT
EVERHTKVID TWTETNERLV DAVKKNFNQN DPLNSVWMMA NSGARGNMSQ VRQLVGMRGL
MANPQGEIID LPIRTNFREG LTVTEYVISS YGARKGLVDT ALRTADSGYL TRRLVDVAQD
VIVREDDCGT SRCILVKAED GKYGNRLVGR LTADQVVGAD GEVLAERNTE IDPPLSKRFE
KAAVQAVSVR SPLTCEANRS VCRKCYGWAL AHNELVDLGE AVGIIAAQSI GEPGTQLTMR
TFHTGGVSTA ETGVVRSKLE GTVEFGAKAR VRPYRTPHGV NAQQAEVDFN LTIQPSGKGK
PQKIEITNGS LLFVDNGQAI DADVTVAQIA AGAVKKSVEK ATKDVICDLA GQVSYDPSIQ
PREVTDRQGN ITHKAQRLGR MWVLAGDVYN LPPNARPVVT AGATVTEGQV LAEASQASEY
GGAIRLREAL GDSREVQIVT TAMTLRDFKL QGESTHAGEI WNLEAKDGTR YRLNTIPGSK
IGSGEVVAEL NDDRFRTQTG GLVRFAPGLA IKKARSAKNG YEVNKGGTLL WIPQETHEIN
KDISLLMITD GQWIEAGTEV VKDIFSQTAG IVTVTQKNDI LREIIVRSGS FHLCTEKKAL
ERFQGDGVMV NPGEPIAKGI STETMVYVQT VETPEGSGLL LRPVEEYTIP NEAQLPDLGH
VKQPNGPHLG LKASQRLAFK DNELVKSVEG VELLRTQLML ETFDTTPQMT VDVEAVPDKR
AKTIERLQLV ILESILVRRD TISDSSHGST HTELQVEDGQ SIKAGEVIAT TQILCKQEGV
AQMPEATADE PVRRLIVERP EDTLTISTNS QPVVTVGQRI VDGEELAAGQ PSDCCGEVEK
VDSTSVTLRL GRPYMVSPDS LLHVRDGDLV QRGDGLALLV FERQKTGDIV QGLPRIEELL
EARRPRESAI LCKKPGTVEI KQGEDDENTT VTVIEADDAV SEYPILLGRN VMVSDSQQVT
AGELLTDGPI NPHELLECFF EDLRSRKPLM DAAQEAIAKL QHRLVTEVQN VYKSQGVSID
DKHIEVIVRQ MTSKVRVEDA GDTTLLPGEL IELRQVEDTN QAMSITGGAP AEFTPVLLGI
TKASLNTDSF ISAASFQETT RVLTEAAIEG KSDWLRGLKE NVIIGRLIPA GTGFSGFEEE
LKAEAGPHPD ILAEDPAGYR RMQNLRPDYT VDMPAAPAGD ATAVLDDPSD ADMEATRSRH
GIEAGSNFAA FARPDADNEL KEEQVVDAEA VEGLQEEGLL SDE
