RPOB_BUCCC
ID RPOB_BUCCC Reviewed; 1343 AA.
AC Q058E5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=BCc_019;
OS Buchnera aphidicola subsp. Cinara cedri (strain Cc).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=372461;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc;
RX PubMed=17038625; DOI=10.1126/science.1130441;
RA Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M.,
RA Silva F.J., Moya A., Latorre A.;
RT "A small microbial genome: the end of a long symbiotic relationship?";
RL Science 314:312-313(2006).
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; CP000263; ABJ90504.1; -; Genomic_DNA.
DR RefSeq; WP_011672423.1; NC_008513.1.
DR AlphaFoldDB; Q058E5; -.
DR SMR; Q058E5; -.
DR STRING; 372461.BCc_019; -.
DR PRIDE; Q058E5; -.
DR EnsemblBacteria; ABJ90504; ABJ90504; BCc_019.
DR KEGG; bcc:BCc_019; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000669; 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 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; 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..1343
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300288"
SQ SEQUENCE 1343 AA; 153250 MW; BCB0D498C57B4763 CRC64;
MIYSYTEKKR IRENFGKQPK ILDIPYLLSI QIDSFKKFIE PKKNNYQGLE SAFQSIFPIR
SYNGCAELQY VSYTLGKKLF DMYESKTRGT TYSVPLRVKL QLIIYEKDSK NTNVKHIKEQ
EVYMGELPLM THNGTFIING TERVVVSQLH RSPGVFFDSD KGKTHSSGKI LYNARIIPYR
GSWLDVEFDP KDHLFIRIDR RRKIPATVLL HALNFSTEKI LKIFFKHDIF YIKNKNIYMY
LIPKRLKGEI IPFEIIKNKK RYIKKGERIT TEHIKKLKKK KIKTIQIPEE YLYGKTISKN
YYHPKTKEIL IKSNTTLTQD EFNKIKNFNN KKFYVLFTNN IDNGAYISET LKIDTTKDRL
TALIEIYKIM RPGEPPTKEA AENLFNNLFF SQERYDLSPV GRMKFNKSLK RKEKKGSGIL
NKEDIIDVIK KLINIKNGKG EIDDIDHLSN RRVRSVGEMV ENQFRIGLVR VERAVRERLS
LSDLDTLMPQ DIINAKPISS AIKEFFGSSQ LSQFMDQNNP LAEITHKRRI SALGIGGLTR
ERAGFEVRDV HPTHYGRVCP VETPEGPNIG LINSLSIYAR TNQYGFLETP YRKVKNGTVT
TKIKYLSAIE EGNYIIAQAN TKINKFGKFY KKFVTCRYNG EFGLFKNKKV NYMDISTQQI
VSVGASLIPF LEHDDANRAL MGANMQRQAV PTIKSEKPLV GTGMERSVAI DSGVTIIAKR
SGKIEYVDAS RIVVRIKDEK IRTYESGIDI YNLTKYSRSN QNTCINQIPC INLNDSIKKG
DVLADGPSTD LGELALGQNM RVAFMPWNGY NFEDSILISE KVEREDKFTT IHIQELSCIC
RDTKLGIEEI TSDIPNIGES ALSKLDTSGI IYIGADVSSG DVLVGKVTPK GETQLTPEEK
LLRAIFGEKA SDVKDSSLRV PNGTNGTVID VQIFTRDGVK KDKRTIEIEE MLLKKAKKDL
TEELKIFELN IINRINKILL TLKTKINCIV ANSLNEYFKK KIKYPKKIKK KIHTLKIQYK
QLQKKFKKKI KEKTKKIIQG DELAPGILKI VKIFLAVKRK IQPGDKMAGR HGNKGVVSKI
NPVEDMPYDN NGEPIDIVLN PLGVPSRMNL GQILETHLGL AAKGIGNIIN RMLKTNKKIY
KIRKFLQKVY NLGENINQKI NLDNFSDIEI LQLAKNLRIG LPIATPVFDG VNEKEIKKLL
KMSNFSTSGQ ITLFDGRTGE KFERNVTVGY MYMLKLNHLV DDKMHARSTG SYSLITQQPL
GGKAQFGGQR FGEMEVWALE AYGASHTLQE MLTVKSDDVT GRTKMYKNIV SGKHNMEPGM
PESFNVLVKE IRSLGINIEL NNN
