RPOC2_SYNJA
ID RPOC2_SYNJA Reviewed; 1302 AA.
AC Q2JQT4;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=CYA_0411;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
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; CP000239; ABC98630.1; -; Genomic_DNA.
DR RefSeq; WP_011429319.1; NC_007775.1.
DR AlphaFoldDB; Q2JQT4; -.
DR STRING; 321327.CYA_0411; -.
DR EnsemblBacteria; ABC98630; ABC98630; CYA_0411.
DR KEGG; cya:CYA_0411; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000008818; 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..1302
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353538"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1302
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 1302 AA; 142990 MW; 0BC2499357FA563D CRC64;
MSEKGRFSAG LVRQAADGAK AKTPPPPVPF RNYQIGKKEL RNLIAWSFAR YGTARTAQMA
DALKALGFKY ATQAAVSISI EDLRIPPSKR QLLAQAEAEI EAATERYTRG EITEVERYQK
VIDTWNQTND QIKEEMLSNF RQNDPLNSVY MMANSGARGN VSQVRQLVGM RGLMANPQGE
IIDLPIKTNF REGLTVTEYI ISSYGARKGL VDTALRTADS GYLTRRLVDV SQDVIVRESD
CGTDQGILLE PLMDADKVVV SLEERLVGRV LARDVVHPQT QEILARRNQE VDHDLAKAIV
EAGIRQVMVR SPLTCEANRS VCRMCYGWSL AHSRLVDLGE AVGIIAAQSI GEPGTQLTMR
TFHTGGVFTG EVARQIRAPF AGVVRFPKNL RTRPFRTRHG DDALQLEANN QIVLEGPDGQ
REVFDMTQGS TLLVRDGAQV QRDQLIAEVT VAKAVRKSTE KAQKEVVADL AGEIRFADLP
IEEKTDRQGN TTCTAQRQGL IWVMSGQVYN LPPGAEPVVK NGDRVQAGDV IAETSLVTEH
GGIVRLPERS DTKSGREVEI INAAVVLHEA RVRVESHQGR EQFLLDTASG QTFVLKATPG
TKVGNDEVVA ELIENNFRTQ TGGLVKFAGV EVARRGKAKQ GYEVIRGGTL LWIPEETHEV
NKDISLLNVE DGQYVEAGTE VVKDIFCQNA GVVEVIQKND ILREIVIKPG SLHLVDDPAD
LEIPTGTLIQ PGQKLLSSIV PDRLVYLEQV ETPEGPGLLL RPVYEYEIPD RPVVPSQEST
SESGRSIRLR AVQRVPFKDG ERVKSVGPVE LLRTQLVLEI DTDAPQLKAD IELIQDEKDP
SIRRLQLVIL ETLLLRRDVE ADLTQGSTHT RLLVSEGDSI GRGGVIARTE IQAKKAGIVQ
GIRQGAEVVR RVLVVTDDDL LTVPLTGQAS VEVGALVRAG DELAPGIPAP ESGQVMQIAD
GQVVLRLARP YLVSAGAILQ VRDGDLVQRG DSLALLVFER AKTGDIIQGL PRIEELLEAR
KPKEMCVLAK RPGTVQLSWR GEEPDLRVIE ADGTVTEYSV MPGQNLIVVD GQPVQVGDPL
TDGPANPHDL LEIYFEYHRQ TLGDDQAARL ALREVQRFLV NEVQNVYRSQ GVEIADKHIE
IVVRQMTSKV RVDDSGDTVL LPGELVELRE IQQTNATMAI TGGAPAKYTP VLLGITKASL
NTDSFISAAS FQETTRVLTE AAIEGKSDWL RGLKENVIIG RLIPAGTGFS TYEEMAPEPE
PEEEEEPVVL PELPPRLILD DDQLIDDSTP VDEPTEDEGE EE
