RPOC2_PROM0
ID RPOC2_PROM0 Reviewed; 1366 AA.
AC A3PEX2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=P9301_16741;
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301;
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}.
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DR EMBL; CP000576; ABO18297.1; -; Genomic_DNA.
DR RefSeq; WP_011863594.1; NC_009091.1.
DR AlphaFoldDB; A3PEX2; -.
DR STRING; 167546.P9301_16741; -.
DR EnsemblBacteria; ABO18297; ABO18297; P9301_16741.
DR KEGG; pmg:P9301_16741; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR Proteomes; UP000001430; 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..1366
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353527"
FT REGION 1..34
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 1291..1307
FT /note="Polar 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; 149722 MW; 1A92CE5F319B5B76 CRC64;
MTSSKPKKTS RVRKTTKNSK KNNPLTMPAL AKTPPSFKNK VVDKKALKNL VSWAYKTHGT
AVTAAMADNL KDLGFKYATQ AAVSISVDDL KVPEAKQDLI GQAEEQISAT EECYRLGEIT
EVERHTKVID TWTETNERLV DAVKNNFNQN DPLNSVWMMA NSGARGNMSQ VRQLVGMRGL
MANPQGEIID LPIRTNFREG LTVTEYVISS YGARKGLVDT ALRTADSGYL TRRLVDVAQD
VIVREEDCGT ERSIVVEAED GKFGARLLGR LTAEDIFDAE ENLVVPQNTA IDPALSGEIE
KASINKVKIR SPLTCEANRS VCRRCYGWAL AHNHLVDLGE AVGIIAAQSI GEPGTQLTMR
TFHTGGVSTA ESGVVRSKIT GKVEFSSKAK VRGYRTPHGV EAKQAEVDFI LKIVPQGSNS
GKPQKIEVSS GSLLFVEDGE EINSDITVAQ IIAGTVKKSV EKATKDVICD LAGQVRYDKV
IQPKEVTDRQ GNITLKAQRL GRLWVLAGDV YNLPPNARPV ISSGKSVDEG TVLAEASQSS
EFGGQVRLRE SVGDSREVQI VTTSMSLTNF KLIEESTHSG QIYNLESSDG ISYRLNISPG
SKISNGEVIA DLTDERFRTK TGGLVKYAPG LSVKKARSSK NGFEVSQGGT LLWIPQETHE
INKDISLLMI EDMKWIEAGT EVVKDIFSQT SGIVTVTQKN DILREITVRN GTFHECDDEE
VLNRFTEEGN LVNPGEKILD GVDNKEILFV QKLETPKCRG LLLRTVEEFT IPDQAELPQL
SHVKQEKGPH LGLKAIQRLT YKDGELIKSV EGVELLRTHL SIESFDATPQ MTIDVESIED
KNDASINRLN LVILESILVR RDTLSDSSHG STHTELQVKN DQLVKAGDVI ATTQILCKEK
GFVQLPNVVE DEPIRRLIVE REEDKIKIKI SDKAVVKIGD RVVDGDPISK SVKSTSCGEI
EEISNSSVTL RLGRPYMVSP DSVLHVKDGD LVLRGDGLAL LVFERQKTGD IVQGLPRIEE
LLEARRPRDS AILSKKSGIV QIKKGNDEES VSLSVIEKDD FVNEYQLLIG KNIMVSDGQQ
VTGGESLTDG PINPHELLDC YFNDLKDQKP LIEAARESIS KLQRSMVSEV QNVYKSQGVA
IDDKHIEVIV RQMTSKVRIE DAGDTTLLPG ELIELRQVED TNQAMAITGG APAEFTPVLL
GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFSGFV
EELSSEAGPH PDILAEESGG YRRAQNLRPD YTVDMPQSPS VSSTAILDDP SDEDLETTRN
RHGIDPSSSN FAAFARPNAE NQFSEDQLPD PAALEGLQEE GLLSDE
