RPOB_HAMD5
ID RPOB_HAMD5 Reviewed; 1341 AA.
AC C4K4F1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=HDEF_0711;
OS Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX NCBI_TaxID=572265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5AT;
RX PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT "Hamiltonella defensa, genome evolution of protective bacterial
RT endosymbiont from pathogenic ancestors.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(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}.
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; CP001277; ACQ67444.1; -; Genomic_DNA.
DR RefSeq; WP_015873265.1; NC_012751.1.
DR AlphaFoldDB; C4K4F1; -.
DR SMR; C4K4F1; -.
DR STRING; 572265.HDEF_0711; -.
DR PRIDE; C4K4F1; -.
DR EnsemblBacteria; ACQ67444; ACQ67444; HDEF_0711.
DR GeneID; 66260564; -.
DR KEGG; hde:HDEF_0711; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002334; 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; 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..1341
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000214480"
SQ SEQUENCE 1341 AA; 150447 MW; B5549ED83498EBC9 CRC64;
MVYSYTEKKR IRKNFGKRPQ VLDIPYLLSI QLDSFQKFIE QDPKGQQGLE AAFRSVFPIQ
SYSAHSELQY VNYRLGEPVF DVKECQIRGA TYSAPLRVKL RLVVYEKEAP EGTVKDIKEQ
EVYMGEIPLM TENGTFVVNG TERVVVSQLH RSPGVFFDSD KGKTHSSGKV LYNARVIPYR
GSWLDLEFDP KDNLFVRIDR RRKLPATIIL RALDYSTTDI LNLFFEKVRF EICNDKLEMN
LVPERLRGET ASFDIQINGK IYVEKGRRVT ARHIRQLDKD QIQRIEVPVE YIIGKVVAQD
YIDENTGELI CSANTELSFD LLAKLSQAGH QQIETIFTND LDHGDYISQT LKVDPTTDRL
SALVEIYRMM RPGEPPTREA AENLFENLFF SEERYDLSAV GRMKFNRSLL RDEIEGSGIL
SKEDIIEVMK KLIGIRNGKG EIDDIDHLGN RRIRSVGEMA ENQFRIGLVR VERAVKERLS
LGDLDTLMPQ DMINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR
ERAGFEVRDV HPTHYGKVCP IETPEGPNIG LINSLSVYAC TNEYGFLETP YRSVHEGAVT
NEIHYLSAIE EGNFVIAQAN SNLDDNGYFI EDLVTCRNKG ESSLFRKEQV DYMDVSTQQI
VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLRADKPLV GTGMERAVAV DSGVTCVAKR
GGSVQYVDAS RIVIKVNENE MHPGEAGIDI YNLNKYTRSN QNTCINQIPC INLGELVERG
NVLADGPSTD LGELALGQNM RVAFMPWNGY NFEDSILVSE RVMQEDRFTT IQIQELACIS
RDTKLGSEEV TADIPNVGEA ALSKLDESGI VYIGAEVNGG DILVGKVTPK GETQLSPEEK
LLRAIFGEKA SDVKDSSLRV PNGVSATVID VQIFTRDGVE KDKRALEIEE MELKQVKKDL
SEELKILEAA LFGRIKAVLI SGGITSEKLS RLPCERWLEL PLSEEQKQEQ LEQLAEQYDE
MKAEFDKKME VKRRKITQGD DLAPGVLKIV KVYLAVKRQI QPGDKMAGRH GNKGVISKIN
PVEDMPYDEE GNPVDIVLSP LGVPSRMNIG QILETHLGMA AKGIGNKINE MLKKNERVSK
LRKFIQKAYD LGDGVCQTVD LSTFSDKEIL SLAENLKKGM TIATPVFDGA KEKEIKQLLK
LADLPTSGQI NLFDGRTGEQ FERPVTVGYM YMLKLNHLVD DKMHSRSTGS YSLVTQQPLG
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GDHRMEAGIP
ESFNVLLKEI RSLGINIELE E
