RPOB_BIFAA
ID RPOB_BIFAA Reviewed; 1186 AA.
AC A1A317;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
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=BAD_1319;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF40100.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP009256; BAF40100.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041777404.1; NC_008618.1.
DR AlphaFoldDB; A1A317; -.
DR SMR; A1A317; -.
DR STRING; 1680.BADO_1407; -.
DR EnsemblBacteria; BAF40100; BAF40100; BAD_1319.
DR GeneID; 56675541; -.
DR KEGG; bad:BAD_1319; -.
DR HOGENOM; CLU_000524_4_3_11; -.
DR Proteomes; UP000008702; 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; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1186
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300284"
FT REGION 1149..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 131478 MW; 07938B8B87A9B156 CRC64;
MAEATTNTTT IIARADQHDI DLHKASDRVN FGSIREPIDV PYLLGVQTDS FDWLIGNERW
QKRVQEDLEN GTNTVPHTSG LDEVFQEISP IENFAQTMSL TFSDPYFEEP RHTVQECKEK
DYTYSAPLYV NAEFENGDTG EIKSQTVFMG DFPLQTPHGT FIIGGTERVI VSQLVRSPGV
YFDRSQDRTS DKEVFGAKII PSRGAWLEFE IDKRDVLGVR VDRKRKQSAI VFLMAIGMTK
DEIADAFKDY PLVMDALAKE TVQTQDEALT DLYRKIRPAD TPTPEAGKNL LDSFYFNTKR
YDLARVGRYK INRKLGLEKD VNDRSLSRED IIATIKYLVT LHAGETKFPG KRDGQDVDLR
VDVDDIDHFG NRRIRQVGEL IQNQLRTGLS RMERVVRERM TTQDPEAITP QSLINIRPVN
ATIKEFFGTS QLSQFMDQNN PLAGVTNKRR LSALGPGGLS RDRASMEVRD VHPSHFGRMC
PIESPEGPNI GLIGSLATFG RINPFGFIET PYRKVVNGHV TDEVEYMTAD RDAEHVIAQA
NQELDENGNF VKKQALARVG EEEAVDVPVS SVDYMDVSPR QMVSVGASLI PFLEHDEGHR
ALMGTNMQRQ AVPLIESERP LVGTGAEWRA AVDSGDVILA EKPGVVTYVS ADIIRTMNDD
GTTSSYKLAK FQRSNQTTCY NQVPLIHDGE RVEAGTVLAD GPATQKGEMA LGKNLLIAFM
PWNGYNYEDA VIISQRLVQD DTLSSIHIEE YEIDARETKL GAEEITRDLP NVGEDAVANL
DERGIIRIGA EVEAGDILVG KVTPKGETEL TPEERLLRAI FGEKSREVRD TSLRVPHGET
GTVIAVKEIT REDAEEDGDE LPNGVNQMIR VYIAQHRKIT QGDKLSGRHG NKGVISRILP
EEDMPFLADG TPVDIMLNPL GVPSRMNLGQ VLELHLGWIA HAGWDISLDP DAEAAWKKYV
PQGAEKGAPG TPVATPVFDG VRPETIKGLL SCTLPDRDGN KLVGPDGKAT LFDGRTGEPF
PKPISVGYMY MLKLHHLVDD KIHARSTGPY SMITQQPLGG KAQFGGQRFG EMEVWALEAY
GAAYTLHEMM TTKSDDVDGR VRVYGAIVKG ENLPPAGIPE SFKVLLKEMQ SLSLNVEVLN
ADGVAIDMKE EDDDPSTSSD DLGFNIGARP DAAAKEDQVA EEPEFQ
