RPOB_RICAH
ID RPOB_RICAH Reviewed; 1373 AA.
AC A8GMA7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=A1C_01010;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) 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; CP000847; ABV74532.1; -; Genomic_DNA.
DR RefSeq; WP_012013402.1; NC_009881.1.
DR AlphaFoldDB; A8GMA7; -.
DR SMR; A8GMA7; -.
DR STRING; 293614.A1C_01010; -.
DR EnsemblBacteria; ABV74532; ABV74532; A1C_01010.
DR KEGG; rak:A1C_01010; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000006830; 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; 1.
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..1373
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000051977"
SQ SEQUENCE 1373 AA; 154164 MW; 5E985474C00E8464 CRC64;
MVSLRDNIEA QPLSHNRRIR KNFGHINLVA DIPNLIEIQK NSYEKNFLQL NIKDSERKNK
GLQSILNSIF PISDSSNIAN LEFVKYEFDT PKYDVEECSQ RSLSYAAPLK VTLRLSIWDI
DEDTGTREIK GIKEQEVYMG DIPLMTKNGT FIINGTERVV VSQMHRSPGV FFYHDEGKVH
SSGKLLYSAR VIPYRGSWLD LEFDAKDVLY FRIDRKRKLY ATTLLRAIGM STEEIIKFYY
NSVTYKLVKK KGWAVKFIPK HITAHRLTSD LVDADTGNVL LKAGQKITPR LAQKYCAEGI
NNILVAHETL IGKYLSEDLR DPASDEVLAK IGEIITSDML NVINDLKIKN VNVLVINPQS
GPYIRNTLFA DKNQDREAAL CDIFRVLRPG EPTNIEAAES LFYNLFFDSE RYDLSEVGRI
KMNSRLGLSI SEEVTVLTID DIKNIVRVLV ELKDGKGIID DIDHLGNRRV RSVGELIENQ
FRIGLVRMEK SVIERMSAGD VDTVMPHDLV NSKILVSVVK EFFSTSQLSQ FMDQTNPLSE
ITHKRRLSAL GPGGLSRDRA GFEVRDVHPT HYGRICPIET PEGQNIGLIN SMATYARINK
HGFIESPYRK VKDGRVIDEV IYLSAIEEGK YKIGQANSKV DRDGKLQGEF INCRVEGGNF
VMVEPHEVDF IDVTPMQVVS VAASLIPFLE NDDANRALMG SNMQRQAVPL IKTDAPFVGT
GVEGVVAKDS GASVLALHDG IVEQVDSNRI VIRTLEQKID GSPSVYIYNL LKFQKSNHNT
CINQKPLVQV GHYVKKNDII ADGPSTDNGE IALGRNVLVA FLPWNGYNFE DSILISERIV
KEDIFTSIHI EEFEVIARDT RLGPEEITRD IPNVSEEALR HLDEVGIIYV GAEVKAGDIL
VGKVTPKSES PITPEEKLLR AIFGEKAFDV KDSSLHVPSG VSGTVVEVRV FSRRGVEKDQ
RAIAIEKQQI EKLAKDRDDE LEIIEHFVFS LLEKLLVGQV IINGLKQVKA GQTITTEMLK
GLSKGQFWQL TVEDANVMNE IEQIKIHYDE KKDALNKRFA TKVEKLQSGD DLPQGALKVV
KVFIATKHKL QPGDKMAGRH GNKGVVSRIV PEEDMPFLED GTVVDIVLNP LGLPSRMNIG
QILETHLGWA SINLAQKIST LVKEYKNKNI GIEKIKKFLL ELYGENINYI LERSEEEIIS
FCNKVGKGVY FATPVFDGAK VQDVKDMLKL AGQDPSGQVK LIDGRTGEYF DRLVTVGQKY
LLKLHHLVDN KIHSRSIGPY SLVTQQPLGG KSHFGGQRFG EMECWALQAY GAAYTLQEML
TVKSDDVNGR IKTYDSIVRG ENNFESGIPE SFNVMIKEFR SLCLNVKLEV TSS