RPOC2_PROMP
ID RPOC2_PROMP Reviewed; 1366 AA.
AC Q7V008;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=PMM1483;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(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; BX548174; CAE19942.1; -; Genomic_DNA.
DR RefSeq; WP_011133111.1; NC_005072.1.
DR AlphaFoldDB; Q7V008; -.
DR SMR; Q7V008; -.
DR STRING; 59919.PMM1483; -.
DR EnsemblBacteria; CAE19942; CAE19942; PMM1483.
DR KEGG; pmm:PMM1483; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000001026; 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_0000067907"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..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 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; 149637 MW; ACF5C5BE90571188 CRC64;
MTSSKPKKSS RVRKTTKNSK KNHNTMMPLL PKTPPSFKNK VVDKKALKNL VSWAYKTHGT
AVTAAMADNL KDLGFKYATQ AAVSISVNDL KVPEAKQDLI GQAEAQITAT EECYRLGEIT
EVERHTKVID TWTETNERLV DAVKNNFNQN DPLNSVWMMA NSGARGNMSQ VRQLVGMRGL
MANPQGEIID LPIRTNFREG LTVTEYVISS YGARKGLVDT ALRTADSGYL TRRLVDVAQD
VIVREEDCGT ERSIVINSED GKFGSRLIGR LSAEDILDSE GNLIVPKNTA IDPSLSKTLE
TSLISKVNIR SPLTCEANRS VCRKCYGWAL AHNHLVDLGE AVGIIAAQSI GEPGTQLTMR
TFHTGGVSTA ESGVVRSKIK GKVEFGSKAK IRGYRTPHGV EAKQAEVDFL LKIIPTGSIT
NKAQKIEVTS GSLLFVEDGQ DIDSDITVAQ ITSGAVKKSV EKATKDVICD LAGEVRYDKV
IQPKEVTDRQ GNITLKAQRL GRLWVLAGDV YNLPPNAKPV VSTETKVEQG TVLAEASQSS
EFGGEVRLRE SVGDSREVQI VTTSMLLSNF KLIEESTHSG ELFHLESNDG TIYRLNTSPG
SKISSGEVIA DLADERFRTK TGGLVKYAPG LSVKKARSSK NGFEVSQGGT LLWIPQETHE
INKDISLLMT EDMEWIEAGT EVVKDIFSQT SGIVTVTQKN DILREITVRN GSFHECEDEE
ILSRFTEEGK LVNPGEKIID GVDNDEILFV QKLETSKGKG LLLRTVEEYT IPNEAELPEL
SHVKQEKGPS LALKAIQRLS YKDGELIKSV EGVELLKTNL SIESFDATPQ MTIDVETIQD
KSDKSINRLN LVILESILVR RDTISDSSHG STHTELQINN NQLVKAGDVI ATTQILCKER
GVLQLPDSVE GEPIRRLIVE RNEDKIKINI KDKAVVKTGD RVVDGDLISK GVKSTSCGEI
EEVSSEYVIL RIGRPYMVSP DSVLHVKDGD LVLRGDGLAL LVFERQKTGD IVQGLPRIEE
LLEARRPRDS SILCKKSGVV QIKEGTDEES VSLSVIERDD SISEYQLLMG QNIMVSDGQQ
VTGGELLTDG PINPHDLLDC LFTDLKDQKP LMEAAQESIS KLQRKMVNEV QNVYKSQGVA
ISDKHIEVIV RQMTSKVRIE DAGDTTLLPG ELIELRQVED TNQAMSITGG APAEFTPVLL
GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFSGFV
EELASEAGPH PDILAEESGG YRRTQNLRPD YTVDMPQTPI VSSTAILDDP SDEDLETTRN
RHGIDPTSSN FAAFARPNAE NQFSEDQLPD PAALEGLQEE GLLSDG
