RPOB_PHATC
ID RPOB_PHATC Reviewed; 1389 AA.
AC A0T0D7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1;
RX PubMed=17252281; DOI=10.1007/s00438-006-0199-4;
RA Oudot-Le Secq M.-P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C.,
RA Green B.R.;
RT "Chloroplast genomes of the diatoms Phaeodactylum tricornutum and
RT Thalassiosira pseudonana: comparison with other plastid genomes of the red
RT lineage.";
RL Mol. Genet. Genomics 277:427-439(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_01321}.
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_01321};
CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC composed of four subunits: alpha, beta, beta', and beta''. When a
CC (nuclear-encoded) sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; EF067920; ABK20635.1; -; Genomic_DNA.
DR RefSeq; YP_874412.1; NC_008588.1.
DR AlphaFoldDB; A0T0D7; -.
DR SMR; A0T0D7; -.
DR STRING; 556484.A0T0D7; -.
DR PRIDE; A0T0D7; -.
DR GeneID; 4524587; -.
DR InParanoid; A0T0D7; -.
DR Proteomes; UP000000759; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..1389
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000276599"
SQ SEQUENCE 1389 AA; 160051 MW; 251B542BB45132EB CRC64;
MNYTNALPDF LAMQRISFCW FITQGLTEEL ALFSRIQDFS QNTEYVMFGE EYSLIKPSYS
LLIARKYSGN YRAQLVIPIE VRNKVVNSIR YHNQFPIITL PLMTTDATFI INGCERVIVS
QIIRSPGVYF EKNKNQKTRN QFKKKLSTDI NKLRSFIPSG EAFISEFDLF FPLPTSIYDP
VKKKKKIIPH WQSNSIYYYS IKYLKQKQQN STFYFLQSFK LYRVASKLLS SKSKQRVIQL
FLKWLKLKNK SFEFQDEKQI YLIKYFNFLL TSLMKYEILQ SSLTTKFNED KTILLSKFTK
SNAILNLSDK QIINLSMIYN KLIINSQTLA QMELNSNLFL ITKEPREWLT EMSNFLFLKK
QISKATFTLK SFQELTQLQN LKPAIYFSIS LKEQLKYVFG KNKLTYKSDR HKYLKTKTQF
LLYRKDHEIK TNYNKKYDEK DLYTATVIPE YGSWIRIGFQ RNTKINSYKY PLKSQEDEVI
IQLDKINQKP VLYLLKEMGL TDLEIYQNLE YADFFYFNKP LLINSKRLSE PLSRFNLGLS
YFKNISEFSR IFDPTYYRLG RVGRLKINSR LNLKMSERLQ TITYEDIFAI TDKLINLTIS
KTVQDDIDHL KNRRVRSVGE LLQNLFRIGF QRLGRKLRNQ TNKIDSGQLL SFNIVNASIR
EFFGSSQLSQ YLDQTNPLSS LTHRRRVSGL GPGGFDRDRI SFAVRDIHPS HYGRICPIET
PEGQNVGLIA SLTTCARVNK SGFLETPFWR VINGKVVKTG QPVYLTADIE DFYKIAPADI
ATNKDNYLTK NVIPVRYKQD FVNVTPSEVD FIAISTIQVV SVAASLIPFF EHDDANRALM
GSNMQRQSVP LLLPQKPIVG TGLENQIAID SGMTLNSYSN GVVSSVTANK IVVNDKTGKR
LTYKLQKYLR SNQQTCINHR PIVWKGEQVK SGQILTDGPA ITSSELSLGQ NVLIGYMPWQ
GYNFEDAILI NERLVYDDVF TSIHIERYKI EIDRNSDTLE RTTKNIPNLN PREIRHLNDD
GIVTVGTFVR PGDILVGKVI SNNTSEQLPE SKLLRAIFGA KAKGVKDNSY RMSDGEYGRV
IETVTFNRRT KLTYKFEKIY VFIAQIRKIQ VGDKIAGRHG NKGIISRILS RQDMPFLPDG
TPLDILLNPL GVPSRMNVGQ LYECLLGLAG DKLNARFKIL PFDEMYGLEI SRILINKKLR
QASIAKNESW LFNPYAPGKM VLIDGRTGKE FENPVTVGNA YMLKLIHLVD DKMHARATGP
YSLITQQPLR GKAQHGGQRF GEMEVWALEG FGAAFTLKEL LTIKSDDMQG RNETLNAIVK
GQQIPKFGIP ESFKVLLHEL RSIGLDMSTY KINRFNSTKR YEVEVNLIEK YNALSKTFSP
TSNINDISF
