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RPOB_STRZJ
ID   RPOB_STRZJ              Reviewed;        1203 AA.
AC   C1CGP4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN   Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=SPJ_1954;
OS   Streptococcus pneumoniae (strain JJA).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=488222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JJA;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR   EMBL; CP000919; ACO18376.1; -; Genomic_DNA.
DR   RefSeq; WP_000907151.1; NC_012466.1.
DR   AlphaFoldDB; C1CGP4; -.
DR   SMR; C1CGP4; -.
DR   EnsemblBacteria; ACO18376; ACO18376; SPJ_1954.
DR   KEGG; sjj:SPJ_1954; -.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000002206; 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: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; -; 2.
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; 2.
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   TIGRFAMs; TIGR02013; rpoB; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW   Transferase.
FT   CHAIN           1..1203
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000165827"
FT   REGION          1174..1203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1203 AA;  134362 MW;  6804DC30A553B859 CRC64;
     MAGHDVQYGK HRTRRSFSRI KEVLDLPNLI EIQTDSFKAF LDHGLKEVFE DVLPISNFTD
     TMELEFVGYE IKEPKYTLEE ARIHDASYSA PIFVTFRLIN KETSEIKTQE VFFGDFPIMT
     EMGTFIINGG ERIIVSQLVR SPGVYFNDKV DKNGKVGYGS TVIPNRGAWL ELESDSKDIT
     YTRIDRTRKI PFTTLVRALG FSGDDEIFDI FGDSELVRNT VEKDIHKNPM DSRTDEALKE
     IYERLRPGEP KTAESSRSLL VARFFDPRRY DLAAVGRYKI NKKLNVKTRL LNQTIAEPLV
     DPETGEILVE AGTIMTRSVI ESIESHLDGD LNKIVYIPND AAVVTEPVVL QKFKVIAPTD
     PDRVVTIIGN ANPDDKVRTV TPADILAEMS YFLNLAEGLG RVDDIDHLGN RRIRAVGELL
     ANQVRLGLSR MERNVRERMS VQDNEVLTPQ QIINIRPVTA AVKEFFGSSQ LSQFMDQHNP
     LSELSHKRRL SALGPGGLTR DRAGYEVRDV HYTHYGRMCP IETPEGPNIG LINNLSSYGH
     LNKYGFVQTP YRKVDRETGV VTNEIVWLTA DEEDEYTVAQ ANSRLNEDGT FAEKIVMGRH
     QGVNQEYPAN IVDYMDVSPK QVVAVATACI PFLENDDSNR ALMGANMQRQ AVPLINPQAP
     YVGTGMEYQA AHDSGAAVIA QYDGKVTYAD ADKVEVRRED GSLDVYHIQK FRRSNSGTAY
     NQRTLVKVGD VVEKGDFIAD GPSMENGEMA LGQNPIVAYM TWEGYNFEDA VIMSERLVKD
     DVYTSVHLEE YESETRDTKL GPEEITREIP NVGEDALKDL DEMGIIRIGA EVKEGDILVG
     KVTPKGEKDL SAEERLLHAI FGDKSREVRD TSLRVPHGAD GVVRDVKIFT RVNGDELQSG
     VNMLVRVYIA QKRKIKVGDK MAGRHGNKGV VSRIVPVEDM PYLPDGTPVD IMLNPLGVPS
     RMNIGQVMEL HLGMAARTLG IHIATPVFDG ASSEDLWSTV KEAGMDSDAK TILYDGRTGE
     PFDNRVSVGV MYMIKLHHMV DDKLHARSVG PYSTVTQQPL GGKAQFGGQR FGEMEVWALE
     AYGASNVLQE ILTYKSDDIN GRLKAYEAIT KGKPIPKPGV PESFRVLVKE LQSLGLDMRV
     LDEDDQEVEL RDLDEGMDED VIHVDDLEKA REKAAQEAKA AFEAEEAEKA TKAEATEEAA
     EQE
 
 
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