RPOB_EHRCR
ID RPOB_EHRCR Reviewed; 1380 AA.
AC Q8KWX2; Q2GFP3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 104.
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=ECH_0952;
OS Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=205920;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12710612; DOI=10.1099/ijs.0.02411-0;
RA Taillardat-Bisch A.V., Raoult D., Drancourt M.;
RT "RNA polymerase beta-subunit-based phylogeny of Ehrlichia spp., Anaplasma
RT spp., Neorickettsia spp. and Wolbachia pipientis.";
RL Int. J. Syst. Evol. Microbiol. 53:455-458(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC CRL-10679 / Arkansas;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(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; AF389473; AAM73635.1; -; Genomic_DNA.
DR EMBL; CP000236; ABD45318.1; -; Genomic_DNA.
DR RefSeq; WP_011452916.1; NC_007799.1.
DR AlphaFoldDB; Q8KWX2; -.
DR SMR; Q8KWX2; -.
DR STRING; 205920.ECH_0952; -.
DR PRIDE; Q8KWX2; -.
DR EnsemblBacteria; ABD45318; ABD45318; ECH_0952.
DR KEGG; ech:ECH_0952; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000008320; 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; 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_0000047895"
FT CONFLICT 21
FT /note="L -> I (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 320..321
FT /note="FI -> V (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 325..326
FT /note="LL -> FP (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 355..366
FT /note="EEIFVLNIDFLT -> GNLWFKDGPGI (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..408
FT /note="DTIKAF -> TYKSL (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 412..413
FT /note="LF -> FI (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 417..418
FT /note="ER -> GK (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="G -> S (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 974..977
FT /note="NEIN -> MNH (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="N -> T (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1091..1096
FT /note="PGDKMA -> AQEIKWL (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1100..1102
FT /note="GNK -> VIQ (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1123
FT /note="V -> C (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1130..1134
FT /note="LGVPS -> FGVYLL (in Ref. 1; AAM73635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1380 AA; 155605 MW; 64D4A13E93332157 CRC64;
MSSSVTSTKY VLNSFNSVPR LSYAKSIDIK DSLTDLIKIQ RDSYNAFIGI DQNTESGIKN
IFQSMFPIQD LLGRAVLEFV SYSIGEPQYD EYECIKRGIT FSVPIRIVLR FIVWKVQEVS
FKEVKYVVDE ETSEKSIKYI KEQEVSIGDL PTMTSHGTFI INGIERVIVS QMHRSPGVFF
DSDKGKTYSS GKLIYSARII PYRGSWLDFE FDIKDILYFR IDRKRKLPVS LLLRALGLSN
NDILDTFYDK IRYVKSEKGW VVPFVADRFR GVRLSHDLMD SDGNVLVKAN TRITLRMARK
LANDGLTKYL VPFNEIQGLF IANDLLDSTG NALIISAGEN ITSEHINKLE LFNIEEIFVL
NIDFLTVGPY ILNTLFLDKN VSYEDALFEI YKVLRSGESP SLDTIKAFFD GLFFEKERYD
LSTVGRIKLN DHLGLNVSED ITVLTKDDII HVIKKLVLLR DGEGSVDDID HLGNRRVRSV
GEFIENQFRI GILRLERMIM DYMSSVNFDN AMPCDFVNPK VLATVLKDFF SSSQLSQFMD
QTNPLSEVTH KRRLSALGPG GLTRERAGFE VRDVHPTHYG RICPIETPEG QNIGLISSLA
IYARINKHGF IESPYRKVDK GVVTDKVEYL LAMQESNYYI ADASATLDEN NQFVDDMLYC
RHDGNFVMVK REEVDYIDVS PKQIVSVAAS LIPFLENNDA NRALMGSNMQ RQAVPLLKAD
APLIGTGMES IVAAGSGTVV LAKRGGIVHR VDGLYIVIRA FDQEKNEYLG VDIYNLRKFQ
RSNHNTCINQ RPLVKPGDYV KANDVIADGS AIDQGELALG KNVLVAFMSW QGYNFEDSIV
ISSEVVKKDV FTSIHIEEFE CVVRDTTLGP EKIMRSVPDI NEDSLSHLDD VGIVNVGAEV
SAGDILVGKV TPRPPVSLPP ETKLLVTIFG EKVFDCVDSS LYLPLDVEGT VVDVHVFVRR
GVEENDRSLL IKQNEINGFI KERDYEIDVV SEYFYDELKR VLVSSGVQYN NQNIDDYLAS
IPKKEWWDIN LSDEAMLLQV KDLKEKFDSM IQNAHSKFDQ KIDKLNYGYD LPQGVLCIVK
VFVAVKHNLQ PGDKMAGRHG NKGVISRIVP VEDMPYLEDG TPVDIILNSL GVPSRMNVGQ
ILETHLGWAS VNLGKKIGHI LDNLDELTVS HLRNFLYQVY DGQDLKDNIQ SMSDEDLLVF
AERLRDGVPM AAPVFEGPKD SQISNLLRLA DLDVSGQVDL YDGRIGEKFD RKVTVGYIYM
LKLHHLVDDK IHARSVGPYG LVTQQPLGGK SHFGGQRFGE MECWALQAYG AAYTLQEMLT
VKSDDIVGRV KIYESIIKGD SNFECGIPES FNVMVKELRS LCLDVALKQD KDFLSNEVKD
