RPOB_RHIE6
ID RPOB_RHIE6 Reviewed; 1379 AA.
AC B3PW59;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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};
GN OrderedLocusNames=RHECIAT_CH0001741;
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) 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; CP001074; ACE90711.1; -; Genomic_DNA.
DR RefSeq; WP_012483478.1; NC_010994.1.
DR AlphaFoldDB; B3PW59; -.
DR SMR; B3PW59; -.
DR EnsemblBacteria; ACE90711; ACE90711; RHECIAT_CH0001741.
DR KEGG; rec:RHECIAT_CH0001741; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000008817; 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; Transcription;
KW Transferase.
FT CHAIN 1..1379
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141725"
SQ SEQUENCE 1379 AA; 153505 MW; 29F6125D5D2A7C17 CRC64;
MAQTLSFNGR RRVRKFFGKI PEVAEMPNLI EVQKASYDQF LMVEEPKGGR PDEGLQAVFK
SVFPITDFSG ASMLEFVSYE FEPPKFDVDE CRQRDLTYAA PLKVTLRLIV FDIDEDTGAK
SIKDIKEQSV YMGDMPLMTN NGTFIVNGTE RVIVSQMHRS PGVFFDHDKG KSHSSGKLLF
AARVIPYRGS WLDIEFDAKD IVYARIDRRR KIPVTSLLMA LGMDGEEILD TFYTKSLYKR
DGEGWRIPFK PETLKGAKAI TEMVDADTGE VVVEAGKKLT PRLLRQLSDK GLKALKAGDD
DLYGNYLAED IVNYSTGEIY LEAGDEIDEK TLGIILSNGF DEIPVLGIDH INVGAYIRNT
LSADKNENRQ DALFDIYRVM RPGEPPTMES AEAMFNSLFF DAERYDLSAV GRVKMNMRLD
LTVEDTVRIL RKDDILAVVK MLVELRDGKG EIDDIDNLGN RRVRSVGELM ENQYRLGLLR
MERAIKERMS SIEIDTVMPQ DLINAKPAAA AVREFFGSSQ LSQFMDQVNP LSEITHKRRL
SALGPGGLTR ERAGFEVRDV HPTHYGRICP IETPEGPNIG LINSLATFAR VNKYGFIESP
YRRIVDGKVT NDVLYLSAME EAKYYVAQAN AEMNPDGSFV DEFVVCRHAG EVMLAPRDSM
NLMDVSPKQV VSVAAALIPF LENDDANRAL MGSNMQRQAV PLLRAEAPFV GTGMEPVVAR
DSGAAIGARR GGVVDQVDAT RIVIRATEDL EAGKSGVDIY RLQKFQRSNQ NTCVNQRPLV
TVGDVVNRGD ILADGPSTDL GDLALGRNAL VAFMPWNGYN YEDSILLSER IVADDVFTSI
HIEEFEVMAR DTKLGPEEIT RDIPNVSEEA LKNLDEAGIV YIGAEVQPGD ILVGKITPKG
ESPMTPEEKL LRAIFGEKAS DVRDTSMRMP PGTYGTIVEV RVFNRHGVEK DERAMAIERE
EIERLAKDRD DEQAILDRNV YGRLIDMLRG QVSIAGPKGF KKGTELSNAV VSEYPRSQWW
MFAVEDEKVQ SELEALRGQY DESKSRLEQR FMDKVEKVQR GDEMPPGVMK MVKVFVAVKR
KIQPGDKMAG RHGNKGVVSR IVPVEDMPFL EDGTHVDVVL NPLGVPSRMN VGQILETHLG
WACAGMGRQI GELIEAYKAN GNIEPLRKTI GDVVGAGPKA EQVHEFDDDS VLRLADQWKR
GVSIATPVFD GANEGDVNDM LRLAGLKDTG QSTLYDGRTG EQFDRQVTVG YIYMLKLNHL
VDDKIHARSI GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL EAYGAAYTLQ EMLTVKSDDV
AGRTKVYEAI VRGDDTFEAG IPESFNVLVK EMRSLGLSVE LENTKLDEAQ ANQLPDAAE
