RPOC2_PROM9
ID RPOC2_PROM9 Reviewed; 1366 AA.
AC Q318Q9;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=PMT9312_1576;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000111; ABB50636.1; -; Genomic_DNA.
DR RefSeq; WP_011377118.1; NC_007577.1.
DR AlphaFoldDB; Q318Q9; -.
DR SMR; Q318Q9; -.
DR STRING; 74546.PMT9312_1576; -.
DR EnsemblBacteria; ABB50636; ABB50636; PMT9312_1576.
DR KEGG; pmi:PMT9312_1576; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000002715; 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 Transcription; Transferase; Zinc.
FT CHAIN 1..1366
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353529"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..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; 149295 MW; 8C0DDD8350FB5E80 CRC64;
MTSSKPKKTS RVRKTTKNSK KNIPLTMPPL AKTPPSFKNK VVDKKALKNL VSWAYKTHGT
AITAAMADNL KDLGFKYATQ AAVSISVDDL KVPAAKQDLI GQAEEQISAT EECYRLGEIT
EVERHTKVID TWTETNERLV DAVKDNFNQN DPLNSVWMMA NSGARGNMSQ VRQLVGMRGL
MANPQGEIID LPIRTNFREG LTVTEYVISS YGARKGLVDT ALRTADSGYL TRRLVDVAQD
VIVREEDCGT ERSIVVEAED GKFGARLLGR LTAEDILDSE EKLIIPQNTA IDPALSGKIE
TASITKVKIR SPLTCEANRS VCRRCYGWAL AHNHLVDLGE AVGIIAAQSI GEPGTQLTMR
TFHTGGVSTA ESGVVRSKIS GRVEFSSKAK VRGYRTPHGV EAKQAEVDFI LKIVPQGNNS
NKSQKVEVSS GSLLFVDDGE EISSDITVAQ IIAGAVKKSV EKATKDVVCD LAGQVKYDKV
IQPKEVTDRQ GNITLKAQRL GRLWVLAGDV YNLPPNARPV VSSGKSVVEG TVLAEASQSS
EFGGQVRLRE SVGDSREVQI VTTSMSLNNF KLIEESTHSG QIYNLESSDG TLYRLNTAPG
SKVSNGQVIA DLTDERFRTK TGGLVKYSPG LSVKKARSSK NGFEVSQGGT LLWIPQETHE
INKDISLLMT EDMKWIEAGT EVVKDIFSQT SGIVTVTQKN DILREITVRN GTFHECDDEE
VLNRFTEEGN LVNPGEKILD GIDNKEILFV QKLETSKGRG LLLRTVEEFN IPDQAQLPNL
SHVKQEKGPH LGLKAIQRLT YKDGELIKSV DGVELLRTHL SIESFNATPQ MTIDVESMED
ENDASINRLN LVILESILVR RDTMSDSSHG STHTELQVKN NTLVKAGDVI ATTQILCKEK
GLVQLPNVVE DDPIRRLIVE REEDKIKIKI SNKAVVKVGD RVVDGDPISG SEKAISCGEI
EEVSSSSVTL RIGRPYMVSP DSVLHVEDGD LVLRGDGLAL LVFERQKTGD IVQGLPRIEE
LLEARRPRDS AILCNKSGVV QIKQGNDEES VSLSVIEKDD LVNEYQLLPG KNIMVSDGQQ
VTGGEVLTDG PINPHELLDC YFSDIRDQKP LIDAARESIS KLQRSLVNEV QNVYKSQGVA
IDDKHIEVIV RQMTSKVRIE DAGDTTLLPG ELIELRQVED TNQAMAITGG APAEFTPVLL
GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFSGFV
EELASEAGPH PDILAEESGG YRRAQNLRPD YTVDMPQSPA VSSTAILDDP SDEDLETTRN
RHGIDPSSSN FAAFARPSAE NQFSEDQLPD PAALEGLQEE GLLSDE
