RPOB_TROWT
ID RPOB_TROWT Reviewed; 1157 AA.
AC Q93GF2;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 122.
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=TWT_071;
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=203267;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11427549; DOI=10.1128/jcm.39.7.2425-2430.2001;
RA Drancourt M., Carlioz A., Raoult D.;
RT "rpoB sequence analysis of cultured Tropheryma whippelii.";
RL J. Clin. Microbiol. 39:2425-2430(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist;
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
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=AAL05611.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAO44168.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF243072; AAL05611.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014184; AAO44168.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q93GF2; -.
DR SMR; Q93GF2; -.
DR STRING; 203267.TWT_071; -.
DR EnsemblBacteria; AAO44168; AAO44168; TWT_071.
DR KEGG; twh:TWT_071; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002200; 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..1157
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047990"
FT CONFLICT 693
FT /note="D -> H (in Ref. 1; AAL05611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1157 AA; 127880 MW; DB8DCE2EEFD000E5 CRC64;
MSLFGVGFLA SAKGKRVCAI GRSSLGKISD PLEVPNLLDL QLDSFDWLIG GPRWRVALDA
YRKNPSGAPI AEKSGLDEVF DEISPIEDSA GNMQLNFSKP VLEAEELSVR ECRVRGRTYS
APLYVEAEFM NHDTGEIKTQ TVFMGDFPLM TDKGTFVING TERVVVSQLV RSPGVYFERT
PEKNSEKDLF SGRIIPARGA WLEFEVDRHD QLGVRVDRKR RQPVIFFLRA IGMTDDEIRD
AFGEFESISV QHEKNIGLSR DDALREIYRR VRPGEQASAE AGRALLENFY FTSRRFDLAR
VGRYKVNRKL GVDVDPTRMV LTRSDIIATI RYLAALHLGF SEVAVLNSNK SVPISTDDID
HLGNRRIRPV GELVQNQLRA GLARMERVVR ERMTTQDIEA IIPQTLINVM PIVAALKEFY
GTSQLSQFMD QNNPLAGLTH KRRLSALGPG GLSRERAGVE VRDVNPSHYG RMCPIETPEG
PNIGLIGSLA CYSRVNSFGF IETPYRRVVN GKVTDDIEYM TATQEDEHAI AQASTPLRPD
NSFVDERVLV RRKGGEVEVV PADQVDYMDV SGRQMVSVAT SLIPFLEHND ANRALMGSNM
QRQAVPLLVT ESPLVGTGME RYVAIDAGDV LIAEDPGIVG DVSADVVTVK QDDGKHRDYH
VGKFVRSNQG NCYNQRVVVR SGDRVEKGTV LADGPCTDKG ELSLGRNLLV AFMPWEGYNF
EDAIIISQNL VKDDTLSSIH IEEHEVSTRD TKLGSEEITR DLPNVSMDYI KDLDERGIIR
IGAEVGPGDI LVGKVTPKGE TELSAEERLL RAIFNEKSME VRDTSLKVPH GQQGTVIDVK
LFDAVDGEDK LGAGINQRVV VYIAHKRKIT EGDKLAGRHG NKGVISKILP VEDMPFMADG
TPVDIILNPL GVPARMNFGQ VLETHLGWIS KQGWKIEGDP DWAKDIRVRE AQPDSRVSSP
VFDGISEGEI TGLFSSVFPN RDGERAVGSD GKAILYDGRT GEPFPEPISV GYMYVLKLHH
LVDDKIHARS TGPYSMITQQ PLGGKAQFGG QRFGEMEVWA LEAYGAAHAL QELLTIKSDD
VVGRVKVYDA IVKGYPIPTP GVPESFKVIV KEMQSLCINI EVVSDGEDDV SADAETLQIE
EGLDTSPKVE VGSLEEV
