RPOB_EHRCJ
ID RPOB_EHRCJ Reviewed; 1380 AA.
AC Q3YST5;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Ecaj_0169;
OS Ehrlichia canis (strain Jake).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake;
RX PubMed=16707693; DOI=10.1128/jb.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(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}.
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; CP000107; AAZ68220.1; -; Genomic_DNA.
DR RefSeq; WP_011304298.1; NC_007354.1.
DR AlphaFoldDB; Q3YST5; -.
DR SMR; Q3YST5; -.
DR STRING; 269484.Ecaj_0169; -.
DR PRIDE; Q3YST5; -.
DR EnsemblBacteria; AAZ68220; AAZ68220; Ecaj_0169.
DR KEGG; ecn:Ecaj_0169; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000435; 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; 2.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1380
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224054"
SQ SEQUENCE 1380 AA; 155495 MW; A9F4B74AE87C6319 CRC64;
MSSSVTPTKY VLNSFNSVPR LSYAKSIDIK DSLTDLIKIQ RDSYNAFIGV GQNTESGIKN
IFESMFPIED LLGRAVLEFV SYSIGEPQYD EYECIKRGIT FSVPIRIVLR FIVWKVQEVS
FKEVKYVVDE ETSEKSIKYI KEQEVSIGDL PTMTPHGTFI INGIERVIVS QMHRSPGVFF
DSDKGKTYSS GKLIYSARII PYRGSWLDFE FDIKDILYFR IDRKRKLPVS LLLRALGLSN
NDILNTFYDK IRYVKCEKGW IVPFVVDRFR GVRLSHDLVD VNGNVLVKAN TRITLRMAKK
LANDGLTEYL VPFAEIQGLF IANDLFDPSG NALIISAGEN ITSEHINKLE LFDIKEIFVL
NIDFLTVGPY ILNTLFLDKN VTYEDALFEI YKVLRSGESP SLDTIKAFFD GLFFEKERYD
LSTVGRIKLN DHLGLNVSED ITVLTKDDII HVIKKLVLLR DGEGSVDDID HLGNRRVRSV
GEFIENQFRI GILRLERMIM DYMSSVNFDN AMPCDFVNPK ILATVLKDFF SSSQLSQFMD
QTNPLSEVTH KRRLSALGPG GLTRERAGFE VRDVHPTHYG RICPIETPEG QNIGLISSLA
IYARINKHGF IESPYRKVDK GVVTDKVEYL LAMQESNYYI ADASATLDEN NQFVDDMLYC
RHDGNFVMVK REEVDYIDVS PKQIVSVAAS LIPFLENNDA NRALMGSNMQ RQAVPLLKAD
APLIGTGMES IVAAGSGTVV LAKRGGIVHR VDGLYIVIRA FDQEKNEYLG VDVYNLRKFQ
RSNHNTCINQ RPLVKPGDYV KANDVIADGS AIDQGELALG KNVLVAFMSW QGYNFEDSIV
ISSEVVKKDV FTSIHIEEFE CVVRDTTLGP EKIMRSVPDI NEDSLSHLDD VGIVNIGAEV
SAGDILVGKV TPRPPISLPP ETKLLVTIFG EKVFDCVDSS LYLPLDVEGT VVDVHVFVRR
GVEENDRSLL IKQNEINGFI KERDYEIDVV SEYFYDELKR VLVNSGVQCN NQNVNDYLES
TPKKDWWNVN LSDETVLLQI NNLREKFDSM IQNAHSKFDQ KIDKLNYGYD LPQGVLCIVK
VFVAVKHNLQ PGDKMSGRHG NKGVISRIVP VEDMPYLEDG TPVDIILNSL GVPSRMNVGQ
ILETHFGWAS VNLGKKIGHI LDNIDELTIS HLRNFLDQVY DGQDLKYNIQ SMSDEDLLAF
AERLRGGVPM AAPVFEGPKD SQISNLLKLA DLDVSGQVDL YDGRIGEKFD RKVTVGYIYM
LKLHHLVDDK IHARSVGPYG LVTQQPLGGK SHFGGQRFGE MECWALQAYG AAYTLQEMLT
VKSDDIVGRV KIYESIIKGD SNFECGIPES FNVMVKELRS LCLDVALKQD KDFLSSEVNN
