ID   RPOB_CUCSA              Reviewed;        1070 AA.
AC   Q4VZP1; A5J1S6; Q2QD97;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 71.
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}; OrderedLocusNames=CsCp018;
OS   Cucumis sativus (Cucumber).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Baekmibaekdadagi;
RX   PubMed=16362300; DOI=10.1007/s00299-005-0097-y;
RA   Kim J.-S., Jung J.D., Lee J.-A., Park H.-W., Oh K.-H., Jeong W.J.,
RA   Choi D.-W., Liu J.R., Cho K.Y.;
RT   "Complete sequence and organization of the cucumber (Cucumis sativus L. cv.
RT   Baekmibaekdadagi) chloroplast genome.";
RL   Plant Cell Rep. 25:334-340(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Borszczagowski;
RX   PubMed=17607527; DOI=10.2478/s11658-007-0029-7;
RA   Plader W.W., Yukawa Y., Sugiura M., Malepszy S.;
RT   "The complete structure of the cucumber (Cucumis sativus L.) chloroplast
RT   genome: its composition and comparative analysis.";
RL   Cell. Mol. Biol. Lett. 12:584-594(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chipper, and cv. Gy14;
RX   PubMed=17546086; DOI=10.1139/g07-003;
RA   Chung S.-M., Gordon V.S., Staub J.E.;
RT   "Sequencing cucumber (Cucumis sativus L.) chloroplast genomes identifies
RT   differences between chilling-tolerant and -susceptible cucumber lines.";
RL   Genome 50:215-225(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; DQ119058; AAZ94643.1; -; Genomic_DNA.
DR   EMBL; AJ970307; CAJ00750.1; -; Genomic_DNA.
DR   EMBL; DQ865975; ABI97409.1; -; Genomic_DNA.
DR   EMBL; DQ865976; ABI98737.1; -; Genomic_DNA.
DR   RefSeq; YP_247591.1; NC_007144.1.
DR   AlphaFoldDB; Q4VZP1; -.
DR   SMR; Q4VZP1; -.
DR   STRING; 3659.XP_004146421.1; -.
DR   PRIDE; Q4VZP1; -.
DR   GeneID; 3429302; -.
DR   KEGG; csv:3429302; -.
DR   eggNOG; KOG0214; Eukaryota.
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; -; 2.
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; 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; 3.
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; 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..1070
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224126"
FT   CONFLICT        912
FT                   /note="A -> AK (in Ref. 2; CAJ00750)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1070 AA;  121039 MW;  D1C82C0A89E65333 CRC64;
     MLGGGNERMS TIPAFNQIQF EGFCRFIDHG LTEELSKFPK IEDTDQEIEF QLFVETYKLV
     EPLIKERDAV YESLTYSSEL YVSAGLIWKT RRDMQEQTIF IGNIPLMNSL GTSIVNGLYR
     IVISQILQSP GIYYRSELDH NGISVYTGTI ISDWGGRLEL EIDRKARIWA RVSRKQKISI
     LVLSSAMGSN LREILENVCY PEIFLSFLND KEKKKIGSKE NAILEFYQQF SCVGGDPVFS
     ESLCKELQKK FFQQRCELGR IGRRNLNQRL NLDIPENNTF LLQRDILAAA DHLIGLKFGM
     GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENMVRGTI CGAIRHKLIP TPQNLVTSTP
     LTTTFESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTASFRI RDIHPSHYGR
     ICPIDTSEGI NVGLIGSLAI HARIGHWGSL ETPFYEISER SKKVRMLYLS PSRDEYYMVA
     TGNSLALNPG IQEEQIVPAR YRQEFLTIEW EQVHLRSIFP FQYFSIGASL IPFIEHNDAN
     RALMSSNMQR QAVPLSRSEK CIVGTGLERQ VARDSGVAAI AEHGGKIIYT DTDKIIFSGN
     GYTRRIPLVM YQRSNKNTCM QQKSQVHQGK CIKKGQILAD GAATVGGELA LGKNVLVAYM
     PWEGYNFEDA VLISERLIYE DIYTSFHIRK YEIQTHVTSH GPERITNEIP HLEARLLCNL
     DKNGIVMLGS WVETGDILVG KLTPQMAKES SYAPEDRLLR AILGIQVSTS KETCLKLPIG
     GRGRVIDVRW IQKKGGSSYN PEIIRVYISQ KREIKVGDKV AGRHGNKGIV SKILPREDMP
     YLQNGRPVDM VFNPLGVPSR MNVGQIFECS LGLAGSLLDR HYRIVPFDER YEQEASRKLV
     FSELYEASKQ TASPWVFEPE YPGKSRIFDG RTGNPFEQPV IIGKPYILKL IHQVDDKIHG
     RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIRARQEVL
     GTTIIGGTIP KPEDTPESFR LLVRELRSLA LELNHFLVSE KNFQINRKEA