RPOB_STRT1
ID RPOB_STRT1 Reviewed; 1193 AA.
AC Q5LXV3;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=str1868;
OS Streptococcus thermophilus (strain CNRZ 1066).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=299768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNRZ 1066;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000024; AAV63382.1; -; Genomic_DNA.
DR RefSeq; WP_002947331.1; NC_006449.1.
DR AlphaFoldDB; Q5LXV3; -.
DR SMR; Q5LXV3; -.
DR KEGG; stc:str1868; -.
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..1193
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224112"
FT REGION 1173..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 133261 MW; 6F748B9E7E287019 CRC64;
MAGHDVQYGK HRTRRSFSRI KEVLGLPNLI EIQTDSFKEF LDTGLKEVFE DVLPISNFTD
TMELEFVGYE LKEPKYTLEE ARIHDASYSA PIFVTFRLIN KETGEIKTQE VFFGDFPIMT
EMGTFIINGG ERIIVSQLVR SPGVYFNDKV DKNGKVGYGS TVIPNRGAWL ELETDSKDIA
YTRIDRTRKI PFTTLVRALG FSGDDEIVDI FGDSELVRNT IEKDIHKNPA DSRTDEALKE
IYERLRPGEP KTADSSRSLL VARFFDPRRY DLAAVGRYKL NKKLNIKTRL LGQTIAENLV
DPETGEILVE AGTEMTRDVI DSIAEHLDGD LNKFVYTPND YAVVTEPVVL QKFKVVAPND
PDRVVTIVGN ANPDDKVRAL TTADILAEMS YFLNLAEGIG KVDDIDHLGN RRVRAVGELL
ANQFRIGLAR MERNVRERMS VQDNEALTPQ QIINIRPVTA AVKEFFGSSQ LSQFMDQHNP
LSELSHKRRL SALGPGGLTR DRAGYEVRDV HYTHYGRMCP IETPEGPNIG LINNLSTYGR
LNKYGFIQTP YRKVDRATGK VTNEVVWLTA DEEDEYIVAQ ANSKLNEDGT FAEEIVMGRH
QGVNQEYPSH LVDFVDVSPK QVVAVATACI PFLENDDSNR ALMGANMQRQ AVPLIDPKAP
FVGTGMEYQA AHDSGAAVIA KHDGKVVYSD ADKVEVRRED GSLDVYTIQK FRRSNSGTAY
NQRTLVKVGD IVEKGDFIAD GPSMEGGEMA LGQNPIVAYM TWEGYNFEDA VIMSERLVKD
DVYTSVHLEE FESETRDTKL GPEEITRELP NVSEEALKNL DEMGIIRIGA EVKEGDILVG
KVTPKGEKDL SAEERLLHAI FGDKSREVRD TSLRVPHGGD GVVRDVKIFT RANGDELQSG
VNMLVRVYIA QKRKIKVGDK MAGRHGNKGV VSRIVPVEDM PYLPDGTPVD IMLNPLGVPS
RMNIGQVMEL HLGMAARNLG IYIATPVFDG ASSEDLWDTV REAGMDSDAK TILYDGRTGE
PFDNRVSVGV MYMIKLHHMV DDKLHARSVG PYSLVTQQPL GGKAQFGGQR FGEMEVWALE
AYGASNILQE ILTYKSDDVN GRLKAYEAIT KGKPIPKPGV PESFRVLVKE LQSLGLDMRV
LDEDDYEVEL RDLDEGEDDD VMHVDDLEKA RVQQAKEAAE LEKAKEEALD KTE
