RPOB_STRPJ
ID RPOB_STRPJ Reviewed; 1203 AA.
AC B8ZNW7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=SPN23F19820;
OS Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=561276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700669 / Spain 23F-1;
RX PubMed=19114491; DOI=10.1128/jb.01343-08;
RA Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA Mitchell T.J.;
RT "Role of conjugative elements in the evolution of the multidrug-resistant
RT pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL J. Bacteriol. 191:1480-1489(2009).
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; FM211187; CAR69733.1; -; Genomic_DNA.
DR RefSeq; WP_000907135.1; NC_011900.1.
DR AlphaFoldDB; B8ZNW7; -.
DR SMR; B8ZNW7; -.
DR KEGG; sne:SPN23F19820; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
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; 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_1000165825"
FT REGION 1174..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1203 AA; 134332 MW; 1EC206F6FAC7AC58 CRC64;
MAGHDVQYGK HRTRRSFSRI KEVLDLPNLI EIQTDSFKAF LDHGLKEVFE DVLPISNFTD
TMELEFVGYE IKEPKYTLEE ARIHDASYSA PIFVTFRLIN KETGEIKTQE 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
