RPOC2_GLOVI
ID RPOC2_GLOVI Reviewed; 1262 AA.
AC Q7NDF7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=glr4278;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC92219.1; -; Genomic_DNA.
DR RefSeq; NP_927224.1; NC_005125.1.
DR RefSeq; WP_011144262.1; NC_005125.1.
DR AlphaFoldDB; Q7NDF7; -.
DR STRING; 251221.35214853; -.
DR PRIDE; Q7NDF7; -.
DR EnsemblBacteria; BAC92219; BAC92219; BAC92219.
DR KEGG; gvi:glr4278; -.
DR PATRIC; fig|251221.4.peg.4306; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR InParanoid; Q7NDF7; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR PhylomeDB; Q7NDF7; -.
DR Proteomes; UP000000557; 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; 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; 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..1262
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067903"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1262 AA; 137588 MW; F71D82D77C33F960 CRC64;
MTQEPQPKFI NRKIDKKGLG KLISWAFSHY GTARTALLAD NLKNLGFRFA TRGAVSISVE
DLQVPDSKVN ILETAEREIQ RAEERFTRGE ITEVERFQKV IDTWAGATQE LTEGVKENFQ
ERNPLNSVGM MAFSGARGNL SQVRQLVGMR GLMANPQGEI IDLPIKANFR EGLNVTEYII
SSYGARKGLV DTALRTADSG YLTRRLVDVS QDVIVREEDC TTQRGIFLGS LRDGDKMIVS
LEERLVGRVA GRDVVHPVTG EVLAPRNTQF DYDSAARIAR SGVDAVMVRS PLTCEANRSV
CRMCYGWSLA HSHLVDIGEA VGIIAAQSIG EPGTQLTMRT FHTGGVFTGE VAKPLKAPFD
GKIKFSSALK ARPMRTRHGD DAYQADQAGT MSLEGSDGKK ETVTITPGSL LLVRDGQRIE
AGTMYAELAL VGKTARKSTE KAQKEVFSDL AGEIKFADLV PEVKTDRQGN ETQYASRLGL
LWVLSGEVYN LPPGAETSLE RGGKVEQGGV IAETRLVTEH GGGVRLKEQD AKGGREVEII
TASVMLDKAI VHEEKSQGRE HYSLETDNGQ VFALKVSPGT KVNNGQVVAE RVDDRYMTKS
GGLIKYSEGV EVAKARGKQG YEVLKGGTLL WIPEETHEVN KDISLLEVED GQYVEAGVQV
VKDIYCLTSG VVAIAQRNDI LREVVIKPGE LHLLDAPSDL KVAHESFAYP GTEVIPGVVT
TDLRYVEQVE TPEGLAVLLR PVEEFPVPDE PDAPSQEASQ QAGSSIRLRG MQRIPYRDGD
RVKAIDGIEL LKTQLVLEIT DQAAQLAADI EFVPDEKDPS MVRLQLVILE TLLIRRDVAA
DLLHGSTLTH ILVKDGERIG PGAIIARTEI LAKQAGTVRG ISRVGQTVRR ILLVTQSDLV
NVPVEGTLTV KPGDLLRAGD KLAKDFASPE SGQVVLAESG RVVVRIGRPY LVSGGAILLV
VDGDLIQRGD NLALLVFERA KTGDIIQGLP RVEELLEGRK PKEMCVLVER PGKVQITQMP
DESYQVSVVE DDGGVTNYPI IGQSLVVVDG QQVQTGESIT DGPSNPHDIL RIFTAREGLQ
KGIESVQRYL VNEVQQVYRS QGVEIHDKHI EIIVRQMTSK VRVEDGGDTT FLPGELVELR
QIEQVNEAMA VTGGAPADCT PVLLGITKAS LNTDSFISAA SFQETTRVLT EAAIEGKSDW
LRGLKENVII GRLIPAGTGF NAYEEAEEVI EDDELIDDTL GLRTVGVAFA GDDDFVEEED
ED
