RPOB_ANAMM
ID RPOB_ANAMM Reviewed; 1382 AA.
AC Q5PBG4;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=AM262;
OS Anaplasma marginale (strain St. Maries).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=234826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St. Maries;
RX PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT is skewed to two superfamilies of outer membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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; CP000030; AAV86365.1; -; Genomic_DNA.
DR RefSeq; WP_011114184.1; NZ_AFMU01000046.1.
DR AlphaFoldDB; Q5PBG4; -.
DR SMR; Q5PBG4; -.
DR PRIDE; Q5PBG4; -.
DR KEGG; ama:AM262; -.
DR HOGENOM; CLU_000524_4_1_5; -.
DR OMA; FMTWEGY; -.
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; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..1382
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224023"
SQ SEQUENCE 1382 AA; 154522 MW; B89B15D1E3DC619D CRC64;
MSSAGGSSGP GYVLNDFDAV PRLSYAKSID IRDSLTDLIR IQRDSYDAFI GIDRDGSSGI
QSIFEAMFPI RDLLGRAVLE FVGYNIGEPQ YDEYECIKRG ITFSVPIRIT LRFVVWKVQE
VSFKEVKYVV DEDTSERSVK YMKEQEVSIG DLPMMTSYGT FIINGIERVI VSQMHRSPGV
FFDSDKGKTY SSGKLIYSAR VIPYRGSWLD FEFDIKDIIY FRIDKKRKLP VSYLLKALGM
SNNDILDAFY DKVIYTRCDK GWRVPFIVDR FKGVRLSYDL MDVDGSVLVK ANTRITLRIA
KKLYADGLRE YMVPFSGITG MFVAADLVDP SSGAVIVSAG ETITSEHIVK LELFDISEIA
FLNIDFLTVG PYVLNTLFLD KNMTQEDALF EIYRVLRSGE SPNLDAVKSF FKGLFFESER
YDLSVVGRIK LNSHLGLDVD ENTTVLTKED IVQVVKKLVL LRDGEGVVDD IDHLGNRRVR
SVGEFIENQF RIGILRLERM IMDYMSSVNF DNAMPCDFVN PKVLATVLKD FFSSSQLSQF
MDQTNPLSEV THKRRLSALG PGGLTRERAG FEVRDVHPTH YGRICPIETP EGQNIGLISS
LAIYAKINKY GFIESPYRKV ENRVVTDKVE YLLAMQEGDY YIADAGAAID ENNRFVDDML
YCRHGGNFVM VKSEDVDYVD VSPKQIVSVA ASLIPFLENN DANRALMGSN MQRQAVPLLK
SEAPLVGTGM EFVVAAGSGA VVLAKRDGIV HRVDGSYIVI RAFDANKDEC LGVDIYRLRK
FQRSNHNTCI NQRPVVKLGD YVKANDVIAD GSAIDRGELA LGKNVLVAFM SWQGYNFEDS
IVISSDVVKR DVFTSIHIEE FECVVRDTPL GPEKIMRSVP DVNEESLSHL DDVGIVNIGA
EVSASSILVG KVTPRPPVSL PPETKLLVTI FGEKVFDCVD SSLYLPPDVE GTVIDVHVFV
RRGVEENDRS LLIKQSEISS FVKERDYEID VVSEYFHDEL RKLLRNAGVK VKGYSDLDSF
FAEASDDTLW STGLADAKVA AKVKDMRERF DSIVGEAHRK FEQKVDKLNY GYDLPQGVLT
IVKVFVAVKH NLQPGDKMAG RHGNKGVISR IVPAEDMPHL EDGTPVDIIL NSLGVPSRMN
IGQILETHLG WAAVNLGKKI GRILDKGGPS MIADLRDFLD KIYDGQKLKS DIASMSSEAL
LVFANRLRKG VPMAAPVFEG PKDAQISKLL ELAEVDPSGQ VYLYDGRLGK KFDRKITVGY
IYMLKLHHLV DDKIHARSVG PYGLVTQQPL GGKSHFGGQR FGEMECWALQ AYGAAYTLQE
MLTVKSDDIV GRVKIYESII KGDSNFECGI PESFNVMIKE LRSLCLNVVL KQDKEFTSGE
VE
