RPOC2_SYNJB
ID RPOC2_SYNJB Reviewed; 1304 AA.
AC Q2JJ17;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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}; OrderedLocusNames=CYB_2438;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(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; CP000240; ABD03372.1; -; Genomic_DNA.
DR RefSeq; WP_011434001.1; NC_007776.1.
DR AlphaFoldDB; Q2JJ17; -.
DR SMR; Q2JJ17; -.
DR STRING; 321332.CYB_2438; -.
DR KEGG; cyb:CYB_2438; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000001938; 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 Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..1304
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353537"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1304
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 241
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 1304 AA; 143665 MW; 3A44FC40E97243DF CRC64;
MSEKGRFSAG LSRQAADGNK ADAPLPPVPF RNYQIGKKEL RNLIAWSFAR YGTARTAQMA
DALKTLGFKY ATQAAVSISV EDLRVPPSKR QLLAQAEAEI EAATERYTRG EITEVERYQK
VIDTWNQIND QIKEEMLNNF RQNDPLNSVY MMANSGARGN VSQVRQLVGM RGLMANPQGR
IIDLPIKTNF REGLTVTEYI ISSYGARKGL VDTALRTADS GYLTRRLVDV SQDVIVRESD
CGTEQGILLE YLMDGDKVVV SLEERLVGRV LARDVVHPQT QEILARRNQE VDHDLARTIA
EAGIRQVMVR SPLTCEANRS VCRMCYGWSL AHSRLVDLGE AVGIIAAQSI GEPGTQLTMR
TFHTGGVFTG EVARQIRAPF AGVVRFPKNL RTRPFRTRHG DDALQVEVNN QIILEGPDGQ
RESFDMTQGS TLLVRDGAQV QRDQLIAEVS LAKASRKSTE KAQKEVVADL AGEIRFADLP
IEEKTDRQGN TTYTAQRQGL IWVMSGQVYN LPPGAEPVVK NGDRVQAGDV IAETSLVTEH
GGIVRLPERS DTRSGREVEI INASVVLREA RVRVESHQGR EQFLLDTSSG QTFVLKATPG
TKVGNDEVVA ELIDNHFRSQ TGGLVKFAGI EVARRGKAKQ GYEVIQGGTL LWIPEETHEV
NKDISLLNVD DGQYVEAGTE VVKDIFCQNA GVVEVIQKND ILREIVIKPG SLHLVDNPAD
LEVKSGTLIQ PGQPVLSSIV PDRLVYLEHV ETPEGPGLLL RPVQEYEIPD RPLVPTQEST
SESGRSIRLR AVQRVPFKDG ERVKSVGPVE LLRTQLVLEI DTDAPQLKAD IELIQDEKDP
DIRRLQLVIL ETLLLRRDVE ADLTQGSTHT RLLVKEGDSI ASGDVIARTE IQAKKAGIVQ
GIREGAEVVR RVLVITDDDL VQVPLTGPAN VEVGALVRVG DELAPGIPSP QSGQVMQITD
GQVLLRMARP YLVSAGAILQ VRNGDLVQRG DSLALLVFER AKTGDIIQGL PRIEELLEAR
KPKEMCVLAK RPGTVQLSWR GEEPDLKVIE ADGTVRDYSV LPGQSLIVVD GQPVGVGDPL
TDGPANPHDL LEIYYEYHRQ TLGDDQAARL ALREVQRFFV NEVQNVYRSQ GVEISDKHIE
IVVRQMTSKV RVDDGGDTIL LPGELVELRE IQQINATMAI TGGAPAKYTP VLLGITKASL
NTDSFISAAS FQETTRVLTE AAIEGKSDWL RGLKENVIIG RLIPAGTGFT TYEEIAAEPE
PDEEEEEPAV LPELPPRLIL EDDQLIDDST PAFDELEEDD DEEE
