RPOC2_PROM5
ID RPOC2_PROM5 Reviewed; 1366 AA.
AC A2BYK9;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=P9515_16631;
OS Prochlorococcus marinus (strain MIT 9515).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167542;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9515;
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; CP000552; ABM72870.1; -; Genomic_DNA.
DR RefSeq; WP_011820963.1; NC_008817.1.
DR AlphaFoldDB; A2BYK9; -.
DR STRING; 167542.P9515_16631; -.
DR PRIDE; A2BYK9; -.
DR EnsemblBacteria; ABM72870; ABM72870; P9515_16631.
DR KEGG; pmc:P9515_16631; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000001589; 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_0000353530"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
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; 149805 MW; DA1FAF4226D60898 CRC64;
MTSSKPKKSS RVRKTSKNSK KNNKIIMPTL AKTPPSFKNK VVDKKALKNL VSWAYKTHGT
AVTAAMADNL KDLGFKYATQ AAVSISVEDL KVPEAKQDLI GQAEAQITST EECYRLGEIT
EVERHTKVID TWTETNERLV DAVKNNFNQN DPLNSVWMMA NSGARGNMSQ VRQLVGMRGL
MANPQGEIID LPIRTNFREG LTVTEYVISS YGARKGLVDT ALRTADSGYL TRRLVDVAQD
VIVREEDCGT ERSIVIEAED GKFGSRLIGR LSAEDVLDSE DNLIIPKNTA IDPSLSKTIE
TSLISTVNIR SPLTCEANRS VCRKCYGWAL AHNHLVDLGE AVGIIAAQSI GEPGTQLTMR
TFHTGGVSTA ESGVVRSKIK GKVEFSSKAK IRGYRTPHGV EAKQAEVDFL LKIIPSGNNS
NKAQKIEVTS GSLLFVDDGQ EIDSDITVAQ ITSGAVKKSV EKATKDVICD LAGQVRYDKV
LQPKEVTDRQ GNITLKAQRL GRLWVLAGDV YNLPPNAKPV ISTEKNVEQG TVLAEASQYS
EFGGEVRLRE SVGDSREVQI VTTSMLLSNF NLIEESTHSG EIFHLESNDG TIYRLNTSPG
SKISSGEVIA DLADERFRTK TGGLVKYAPG LSVKKARSSK NGFEVSQGGT LLWIPQETHE
INKDISLLMT EDMAWIEAGT EVVKDIFSQT SGIVTVTQKN DILREITVRN GSFHECEDEE
VLNRFTEEGQ LVNPGEKIID GVDNNEILFV QKLETSKSKG LLLRTVEEFN IPDEAELPEL
THVKQEKGPS LGLKAIQRLS YKDGELIKSV EGVELLKTHL SLESFDATPQ MTIDVETIKD
KSNDSINRLN LVILESILVR RDTISDSSHG STHTELQVKN NQQVKAGDVI ATTQILCKEK
GIVQLPDLVE NEPIRRLIVE REEDKIKINI TGKALVKVGD RVVDGDSISE GEKATSCGEI
EEVSSKCVTL RLGRPYMVSP DSVLHVKDGD LVLRGDGLAL LVFERQKTGD IVQGLPRIEE
LLEARRPRDS STLCKRSGVV QIKEGNDDES VSLSVIERDD SINEYQLLIG QNIMVSDGQQ
VKGGELLTDG PINPHELLDC LFTDIKDQKP LMDAARESIS KLQRRMVNEV QNVYKSQGVA
IDDKHIEVIV RQMTSKVRIE DAGDTTLLPG ELIELRQVED TNQAMSITGG APAEFTPVLL
GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFSGFV
EELASEAGPH PDILAEESGG YRRAQNLRPD YTVDMPQSPT VSSTAILDDP SDEDLETTRN
RHGIDPSSSN FAAFARPNAE NQFSEDQLPD PAALEGLQEE GLLSDE
