RPOC2_SYNSC
ID RPOC2_SYNSC Reviewed; 1362 AA.
AC Q3AHX7;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Syncc9605_2065;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) 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; CP000110; ABB35805.1; -; Genomic_DNA.
DR RefSeq; WP_011365014.1; NC_007516.1.
DR AlphaFoldDB; Q3AHX7; -.
DR STRING; 110662.Syncc9605_2065; -.
DR EnsemblBacteria; ABB35805; ABB35805; Syncc9605_2065.
DR KEGG; syd:Syncc9605_2065; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
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 Transcription; Transferase; Zinc.
FT CHAIN 1..1362
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353535"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1336
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 1362 AA; 147979 MW; 1D5551292C501E4B CRC64;
MTSSSKSRKS KSSKASKAAK EAPVSASRPL SKTPPPFRNQ VIDKRALKQL VAWSYKNHGT
AVTSSMADNL KDLGFKYATQ AAVSISVDDL KVPEAKKDLL GQAEEQITAT EERYRLGEIT
EVERHTKVID TWTETNERLV DAVKKNFDEN APLNSVWMMA NSGARGNMSQ VRQLVGMRGL
MANPQGEIID LPIRTNFREG LTVTEYVISS YGARKGLVDT ALRTADSGYL TRRLVDVAQD
VIVREDDCGT TRHIVVDAED GKFGSRLVGR LTAAQVVNAD GEVLAERDTE IDPPLSKSFE
AAGVKAVSVR SPLTCEANRS VCRKCYGWAL AHNELVDLGE AVGIIAAQSI GEPGTQLTMR
TFHTGGVSTA ETGVVRSKVA GTVEFGSKAR VRPYRTPHGV NAQQAEVDFN LTIKPSGKGK
AQKIEITNGS LLFVDNGAEI DADVTVAQIA AGAVKKSVEK ATKDVICDLA GQVRYEEAIQ
PREVTDRQGN ITLKAQRLGR MWVLSGDVYN LPPNAQPVVG SETQVTEGQV LAEASQRSEY
GGEVRLRDSI GDSREVQIVT TAMTLKDFKL LEESTHSGEI WNLEAKDGTR YRLNTIPGSK
IGSGEVIAEL ADDRFRTGTG GLVKFAPGLA IKKARSAKNG YEVNKGGTLL WIPQETHEIN
KDISLLMITD GQWIEAGTEV VKDIFSQTAG IVTVTQKNDI LREIIVRSGE FHLCTDAKAL
ERFEGDGQMV NPGEDIAKGL SVDTMKYVQT VETPEGKGLL LRPVEEYTIP NVAQLPELSH
VKQANGPHLG IKATQRLAFK DNELIKSVEG VELLKTQLLL ETFDTTPQMT VDVEKAPDKR
AKTISRLRLV ILESILVRRD TMSDSSHGST HTELQVEDGV SVKAGDVVAT TQILCKQAGL
AQLPEATEAD PVRRMIVERP EDTTTLSTSG KPVVSVGQRI VDGDALAEGE TASCCGEIEA
VSGNSVTLRL GRPYMVSPDS VLHVRDGNLV QRGDGLALLV FERQKTGDIV QGLPRIEELL
EARRPRESTI LCKKPGTVEI KQGEDDESLA VNVIESDDAI GEYPILLGRN IMVSDGQQVT
AGELLTDGPI NPHELLECYF EDLRSRKPLM EAAQEAIANL QHRLVTEVQN VYKSQGVSID
DKHIEVIVRQ MTSKVRVEDA GDTTLLPGEL IELRQVEDTN QAMAITGGAP AEFTPVLLGI
TKASLNTDSF ISAASFQETT RVLTEAAIEG KSDWLRGLKE NVIIGRLIPA GTGFSGFEEE
LQKEAGPHPD ILSEDPAGYR RMQNLRPDYT VDMPPAASAS AVLDDPSDAD LEATRTRHNI
DPSASNFAAF TRPDADNELK EEQVVDAEAV EGLQEEGLLS DE
