RPOC2_PROM2
ID RPOC2_PROM2 Reviewed; 1366 AA.
AC A8G6Y4;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=P9215_17521;
OS Prochlorococcus marinus (strain MIT 9215).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=93060;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9215;
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; CP000825; ABV51365.1; -; Genomic_DNA.
DR RefSeq; WP_012008383.1; NC_009840.1.
DR AlphaFoldDB; A8G6Y4; -.
DR STRING; 93060.P9215_17521; -.
DR PRIDE; A8G6Y4; -.
DR EnsemblBacteria; ABV51365; ABV51365; P9215_17521.
DR KEGG; pmh:P9215_17521; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000002014; 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_0000353526"
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; 149753 MW; 0400E740C0F73FD7 CRC64;
MTSSKPKKTS RVRKTTKNSK KNNPVTMPVL PKTPPSFKNK VVDKKALKNL VSWAYKTHGT
AITSAMADNL KDLGFKYATQ AAVSISVDDL KVPEAKQDLI GQAEEQISAT EECYRLGEIT
EVERHTKVID TWTETNERLV DAVKNNFNQN DPLNSVWMMA NSGARGNMSQ VRQLVGMRGL
MANPQGEIID LPIRTNFREG LTVTEYVISS YGARKGLVDT ALRTADSGYL TRRLVDVAQD
VIVREEDCGT ELSIVVEAED GKFGARLLGR LTAEDIFDAE ENIVVSQNTA IDPSLSEEIE
KASINKVKIR SPLTCEANRS VCRRCYGWAL AHNHLVDLGE AVGIIAAQSI GEPGTQLTMR
TFHTGGVSTA ESGVVRSRIS GKVEFSSKAK VRGYRTPHGV EAKQAEVDFT LKIVPQSNNS
GKAQKIEVSS GSLLFVDDGE EINSDITVAQ ITAGAVKKSV EKATKDVICD LAGQVRYDKV
IQPKEVTDRQ GNITLKAQRL GRLWVLAGDV YNLPPNARPV ISSGKNVDEG TVLAEASQSS
EFGGQVRLRE SIGDSREVQI VTTSMSLTNF KLIEESTHSG QIYNLESSDG TSYRLNISPG
SKINSGEVIA DLTDERFRTK TGGLIKYAPG LSVKKARSSK NGFEVSQGGT LLWIPQETHE
INKDISLLMI EDMKWIEAGT EVVKDIFSQT SGIVTVTQKN DILREITVRN GNFYECDDEE
VLNRFTEEGN LVNPGEKILD GVDNTEILFV QKLETSKCRG LLLRTVEEFT IPDQAELPQL
SHVKQEKGPH LGLKAIQRLT YKDGELIKSV EGVELLRTHL SIESFDATPQ MTIDVESIKD
DKDESINRLN LVILESILVR RDTVSDASHG STHTELQVNN NQLVKAGDVI ATTQILCKEK
GLVQLPNVVD DEPIRRLIVE REQDKIKVKI SDKAVVKVGD RVVDGDPITK TVKSTSCGEI
EEISNSSVTL RLGRPYMVSP DSVLHVKDGD LVLRGDGLAL LVFERQKTGD IVQGLPRIEE
LLEARRPRDS ATLCKKSGIV QIKKGNDEES VSLSVIEKDD LVNEYQLLIG KNIMVSDGQQ
VTGGESLTDG PINPHELLDC YFNDLKDQKP LIDAARESIS KLQRSMVSEV QNVYKSQGVA
IDDKHIEVIV RQMTSKVRIE DAGDTTLLPG ELIELRQVED TNQAMAITGG APAEFTPVLL
GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFSGFV
EELSSEAGPH PDILAEESGG YRRAQNLRPD YTVDMPQSPA VSSTAILDDP SDEDLETTRN
RHGIDPSSSN FAAFARPNAE NQFSEDQLPD PAALEGLQEE GLLSDE
