RPOC2_PROMS
ID RPOC2_PROMS Reviewed; 1366 AA.
AC A2BT59;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=A9601_16871;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000551; ABM70970.1; -; Genomic_DNA.
DR RefSeq; WP_011819098.1; NC_008816.1.
DR AlphaFoldDB; A2BT59; -.
DR SMR; A2BT59; -.
DR STRING; 146891.A9601_16871; -.
DR EnsemblBacteria; ABM70970; ABM70970; A9601_16871.
DR KEGG; pmb:A9601_16871; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000002590; 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..1366
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353524"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1345
FT /note="Polar residues"
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 1366 AA; 149650 MW; F713C7D981FB665E CRC64;
MTSSKPKKTS RVRKTTKNSK KNNPVTMPAL AKTPPSFKNK VVDKKALKNL VSWAYKTHGT
AITAAMADNL KDLGFKYATQ AAVSISVDDL KVPDAKQDLI GQAEEQISAT EECYRLGEIT
EVERHTKVID TWTETNERLV DAVKNNFNQN DPLNSVWMMA NSGARGNMSQ VRQLVGMRGL
MANPQGEIID LPIRTNFREG LTVTEYVISS YGARKGLVDT ALRTADSGYL TRRLVDVAQD
VIVREEDCGT ERSIVVEAED GKFGARLLGR LTAEDVLDAE ENLLVPQNTA IDPALSGEIE
KASINKVKIR SPLTCEANRS VCRRCYGWAL AHNHLVDLGE AVGIIAAQSI GEPGTQLTMR
TFHTGGVSTA ESGVVRSKIS GKVEFSSKAK IRGYRTPHGV EAKQAEVDFI LKIVPQGNNS
GKAQKIEVSS GSLLFVDDGE EINSDITVAQ ITAGAVKKSV EKATKDVICD LAGQVRYDKV
IQPKEVTDRQ GNITLKAQRL GRLWVLAGDV YNLPPNARPV ISSGKSVDEG TVLAEASQSS
EFGGQVRLRE SIGDSREVQI VTTSMSLTNF KLIEESTHSG QIYNLESIDG ISYRLNISPG
SKISNGEVIA DLTDERFRTK TGGLVKYAPG LSVKKARSSK NGFEVSQGGT LLWIPQETHE
INKDISLLMI EDMKWIEAGT EVVKDIFSQT SGIVTVTQKN DILREITIRN GTFHECDDEE
VLNRFTEEGN LVNPGEKILD GVDNKEILFV QKLETPKCRG LLLRTVEEFT IPDQAELPQL
AHVKQEKGPY LGLKAIQRLT YKDGELIKSV EGVELLRTHL SIESFDATPQ MTIDVESIED
KNDSSINRLN LVILESILVR RDTISDSSHG STHTELQVND NQLVKAGDVI STTQILCKEK
GLVQLPNVVD DEPIRRLIVE RQEDKIKIKI SDKALVKVGD RVVDGDPISK SIKSTFCGEI
EEVSNSSVTL RYGRPYMVSP DSVLHVKDGD LVLRGDGLAL LVFERQKTGD IVQGLPRIEE
LLEARRPRDA AILCKKSGIV QIKQGNDEES VSLSVIEKDD LVNEYQLLVG KNLMVSDGQQ
VAGGEPLTDG PLNPHELLDC YFNDLKDQKP LLDAARESIS KLQRSMVSEV QNVYKSQGVA
IDDKHIEVIV RQMTSKVRIE DAGDTTLLPG ELIELRQVED TNQAMAITGG APAEFTPVLL
GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFSGFV
EELSSEAGPH PDILAEESGG YRRAQNLRPD YTVDMPQSPA VSSSAILDDP SDEDLETTRN
RHGIDPSSSN FAAFARPNAE NQFSEDQLPD PAALEGLQEE GLLSDE
