ID   RPOB_HETAK              Reviewed;        1116 AA.
AC   P36440;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 110.
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   Heterosigma akashiwo (Chromophytic alga) (Heterosigma carterae).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Raphidophyceae; Chattonellales;
OC   Chattonellaceae; Heterosigma.
OX   NCBI_TaxID=2829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mangahas J.L., Cattolico R.A., Reynolds A.E.;
RL   Submitted (NOV-1993) 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_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; X75815; CAA53450.1; -; Genomic_DNA.
DR   PIR; S41915; S41915.
DR   AlphaFoldDB; P36440; -.
DR   SMR; P36440; -.
DR   PRIDE; P36440; -.
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; 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; 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   Transcription; Transferase.
FT   CHAIN           1..1116
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048025"
FT   REGION          1070..1116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1070..1098
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1116
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1116 AA;  125819 MW;  EC6C83C81234435B CRC64;
     MVNNTFITKL PDFLEIQRSS FCWFLLKGLS YELNSLSPII DVNVKRVKLK LYPQEFVLKP
     GRTTPICAKQ NDSTYGVRIF LPAEVIYCDT ESKYPTKKNR LEDIKEKVFI GQIPLMTSTG
     SFIVNGCEGY RNQIIRCPGL YYKAEFLNNN IVSTVTIIAQ RGSWLKFEFD KNGYWVRIDK
     EKKISIFDFL EGLNINDEEI LSGLKSIAPL LKYKKTQEIL KRNNDPDLKN LIEKITDPNS
     YSLGIIGRLN LNRRLGLNIS TRVHTLTIHD IFGIIDFFLS ARSFVPDDID DLRNRRIRAV
     GELITSQCEI GLNRLERNIL ERTNFSGSVR ILPKTLVNAR PIMSAIQEFF NSSQLSHYMD
     QTNLLSETAN KRRISALGPG GLNADRVTVA ARDIHPTQYG RLCPIETPEG QNVGLVSTLA
     SYARINRNGF IQTPYFRVEN GKILTQQPLI YLTAEQENLK IAPADVKRDQ DGYLVDDFIV
     TRFQSKNFII TPSKLVDFIS VSEIQIISVA ASLIPFLEHD DANRALMGAN MQRQAVPLLY
     PRKPIVGTGI ESQVAFDSRL VNIATKPGIV KYVSSQQIDI KNIEGEKIAY KLIKYRPSNQ
     DTCLNQRPLV WVGQSIKTGQ VIADGPGTQS GELALGQNLT VAYMPWQGYN YEDAILVSDK
     LDIQNLFTSI HIEECETEVQ QTKTGEQVIT SDIPLVSEKN CKNLDENGII KVGKYVYPGD
     ILVGKITPKG EIDQLPEAKL LKAIFGFKTP DMRDSSLRVP GGLSGRVLDI KIFKKPKPGK
     VFGVGSKIRV FIAQISKLQV GDKIAGRHGN KGVISRILPH QDMPFLPDGT SVDIILNPLG
     VPSRMNVGQI FECLLGLAGD QLNKRFKILP FDEMYQNEAS RILINQKLKD AAKKQNKPWL
     FSAYSPGKIL LSDGRTGEKF DNPVLVGRSY ILKLAHLVED KIHARSTGPY SLITQQPVGG
     KSQNGGQRFG EMEVWALEAF GAAYTLQELL TIKSDDMQGR DDVLNSIVCG QEIPKSSIPE
     SFKVLMRELN ALGLDITTYK VMFENETNKN CLIKNEINLM QTYEEGIKAK IREEEKEREK
     EREAREMEDP EKIVSKIDAK QKKKYKKTKK QTEKKK