RPOC2_THEVB
ID RPOC2_THEVB Reviewed; 1324 AA.
AC Q8DL57;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=tll0640;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC08191.1; -; Genomic_DNA.
DR RefSeq; NP_681429.1; NC_004113.1.
DR RefSeq; WP_011056487.1; NC_004113.1.
DR AlphaFoldDB; Q8DL57; -.
DR SMR; Q8DL57; -.
DR STRING; 197221.22294361; -.
DR EnsemblBacteria; BAC08191; BAC08191; BAC08191.
DR KEGG; tel:tll0640; -.
DR PATRIC; fig|197221.4.peg.679; -.
DR eggNOG; COG0086; Bacteria.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000000440; 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..1324
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067908"
FT REGION 1293..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1324 AA; 144702 MW; 2A82FE2C94B54976 CRC64;
MTEKKPIFFN RIIDKKGLRD LIAWSFSNFG TARTAEMADK IKDLGFHYAT RAGVSISVDD
LLVPPKKQEL LEAAEKEIKT AQERYSRGEI TEVERFQKVI DTWNSTNEEL KNEVVRHFRN
TDVLNSVYMM AFSGARGNLS QVRQLVGMRG LMANPQGEII DLPIKTNFRE GLTVTEYIIS
SYGARKGLVD TALRTADSGY LTRRLVDVSQ DVIIREEDCE TERGITLRSM TVGDKVLALQ
DRLLGRVVLN DVRHPQTGEV LVAKNQAISA DLAKKIVDAG IEEVVVRSPL TCEATGSVCR
LCYGWSLAHA RLVDMGEAVG IIAAQSIGEP GTQLTMRTFH TGGVFTGEVA RQERAPFAGT
VEYGKKLRVR PYRTRHGDDA FIVETAGKLV VKGGQQRQEF DLSQGSIVLV ADGETVAAGQ
LLAEVAQAAR SVRKATEKVT KDVASDLAGQ VKFVNLDAEE KRDRQGTTTR IAPKGGLIWV
LSGEVYNLPP GAEPVVKNGD RIEAGAVLAE TTVKTEHGGV VRLPEQQDSK GGREVEIITA
SVMLDKAKVL KETQQGREHY IIETATGQRF SLKAAPGTKV ANGQVVAELI DDRYHTTTGG
ILKYADIEVA KKGKAKQGYE VLKGGTLLWI PEETHEVNKD ISLLMVEDNQ YVEAGTEVVK
DIFCQNSGVV EVIQKNDILR EIIIKPGELH LVDDPEAARL KHGTLARPGE EVLPGLVVDT
LSQVDYLEDT PEGPAILLRP VQEFSVPDEP SVPSQDSSDG SGQSIRLRAV QRLPYKHDER
VKSVDGVDLL RTQLVLEIGS EAPQLAADIE IVTDEVDPEA QRLQLVILES LIIRRDIAAD
QTQGSTFTSL LVKDGDHIGP GAVIARTDIK AKQAGEVQGI VRSGESVRRI LVVTDSDRLR
VETNGAKPTV KVGDLVRPGD ELAKGVTAPE TAAVMAVADD HVILRLARPY LVSPGAVLQI
EEGDLVQRGD NLALLVFERA KTGDIIQGLP RIEELLEARH PKEKCVLAVR PGTCQVTYNS
DDSVEIKVIE EDGTIQEYPV LPGQNPLVVD GQKVNLADPL TDGPVDPHDI LSIYFEYYKP
QGLLKAAQTS LEKVQSFLVN EVQSVYLSQG IEIADKHIEV IVRQMTSKVR IDDAGDTILL
SGELMTLRQA EQANEPMALT GGAPAQYTPV LLGITKASLN TDSFISAASF QETTRVLTEA
AIEGKSDWLR GLKENVIIGR LIPAGTGFNS YEESSNGDEE WEEGEDRLGQ THVISPEPES
PKMTVNVTAD LGEDVLIDDE TAPHVIEKIT GGARDFEFAS SDVEEDELTE EDDDYGDEEE
EDAF