RPOB_ALKCK
ID RPOB_ALKCK Reviewed; 1180 AA.
AC Q5WLS0;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, 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=ABC0142;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) 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: 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; AP006627; BAD62685.1; -; Genomic_DNA.
DR RefSeq; WP_011245006.1; NC_006582.1.
DR AlphaFoldDB; Q5WLS0; -.
DR SMR; Q5WLS0; -.
DR STRING; 66692.ABC0142; -.
DR EnsemblBacteria; BAD62685; BAD62685; ABC0142.
DR KEGG; bcl:ABC0142; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001168; 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; -; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1180
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224027"
FT REGION 1154..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1180 AA; 132501 MW; 60884E140A705D56 CRC64;
MTGQLIQYGR HRQRRSYARI NEVLELPNLI EIQTASYQWF LDEGLREMFQ DISPIQDFTG
NLVLEFIDYS LGEPKYPVDE SKERDVTFAA PLRVKVRLIN KETGEVKEQE VFMGDFPLMT
ETGTFIINGA ERVIVSQLVR SPSVYYSQKL DKNGKKGFTA TVIPNRGAWL ELETDAKDIV
YVRIDRTRKI PVTVLLRALG FGSDQEIVDL LGENEYLRNT LEKDNTDSTD KALLEIYERL
RPGEPPTVEN AKSLLESRFF DPKRYDLANV GRYKINKKLH IKNRLFNQRL AEKLVDPETG
EVLAEEGTLL DRRTLDKLIP HLEKNVGFRT ARTSGGVLEE SDVEIQSVKI YVADDYEGER
VISVISNGMV ERDVKHIAPA DIIASISYFF NLLHGVGDTD DIDHLGNRRL RSVGELLQNQ
FRIGLSRMER VVRERMSIQD PNVITPQALI NIRPVIASIK EFFGSSQLSQ FMDQTNPLAE
LTHKRRLSAL GPGGLTRERA GMEVRDVHYS HYGRMCPIET PEGPNIGLIN TLSSYAKVNE
FGFMETPYRR VDPETGKVTS RIDYLTADEE DNYVVAQANA KLNDDGSFVD DNIIARFRGE
NTVVPCDRVD YMDVSPKQVV SAATSCIPFL ENDDSNRALM GANMQRQAVP LLVPEAPLVG
TGMEHVSAKD SGAAVVSKYA GIVERVTAKE IWVRRIEEVD GKETKGDLDK YKLQKFVRSN
QGTSYNQRPI VREGDRIEKR EILADGPSME MGEMALGRNV LVAFMTWDGY NYEDAIILSE
RLVKDDVYTS IHIEEYESDA RDTKLGPEEI TRDIPNVGED ALRNLDERGI IRIGAEVKDG
DILVGKVTPK GVTELTAEER LLHAIFGEKA REVRDTSLRA PHGGDGIVLD VKIFNREDGD
ELPPGVNQLV RVYIVQKRKI NQGDKMAGRH GNKGVISRIL PEEDMPFLPD GTPVDIMLNP
LGVPSRMNIG QVLELHLGMA ARKLGIHVAS PVFDGASEED VWGTLEEAGM ARDGKTILYD
GRTGEPFDNR VSVGIMYMIK LAHMVDDKLH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME
VWALEAYGAA YTLQEILTVK SDDVVGRVKT YEAIVKGENV PEPGVPESFK VLIKELQSLG
MDVKMLSSNE EEIEMRELDD EEDQTSEKLN LNLETNESQL
