RPOB_RUTMC
ID RPOB_RUTMC Reviewed; 1360 AA.
AC A1AX75;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Rmag_0811;
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthia.
OX NCBI_TaxID=413404;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
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; CP000488; ABL02532.1; -; Genomic_DNA.
DR RefSeq; WP_011738157.1; NC_008610.1.
DR AlphaFoldDB; A1AX75; -.
DR SMR; A1AX75; -.
DR STRING; 413404.Rmag_0811; -.
DR PRIDE; A1AX75; -.
DR EnsemblBacteria; ABL02532; ABL02532; Rmag_0811.
DR KEGG; rma:Rmag_0811; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002587; 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; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1360
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300393"
SQ SEQUENCE 1360 AA; 151531 MW; 6EFDF76B6C9F5614 CRC64;
MAYSFTEKKR IRNNFGSRES ILTEPDLLAI QIDSFNSFIQ KDSKTKQDIG LHAVFQSVFP
ITAVNGYAQI EYVDYELQEP KFNVEECKLR GVTFASTLRV KLSLVLFDKN GSTLKKKRKI
KQIIEEDIYL GQLPLMTETG TFVINGTERV VVSQLHRSPG VIFEHDKGKT HSSGKILFSS
RIIPYRGSWL DFEYDHHEHL YVRIDRRRKL PVTTLLRAMG LSSEGILETF FEKTTIKLKA
KSCDLNMVPI RLQRTIAEFD IVANQDVIVE KGRRITAKHV KLLKKVGIKS INVPLEYLLD
KVISADIFDK DTGEILISAN TIILEEVLEL LNINKIKKIE ILYINASETG AYISDTLRLD
ETQTEIEARM SIYHVMRPGE PATEDAVNLL FNNLFFKNDR YDLSKVGRMK LNRRLGIGSE
TGEHVLTNDD IISVIKLLIN IKDGNDSVDD VDTLANRRVR AIGEMIENQF RVGLVRVEKV
VREGLNLAET DELTPQDLIN SKPVSAAVRE FFGSSQLSQF MDQVNPLSGV THKRRISALG
PGGLTRERAG FEVRDVHPSH YGRLCPIETP EGPNIGLINT LAVYAKTNSY GFLETPYQVV
KNGKVTKEVV YVSAIDEITH TIAQVNAIVN DKGKLMSDLI SCRHKNEFVL VNSSKVTLID
IDSKQIASVA ASLIPFLEHD DANRALMGSN MQRQAVPVLK AEKPLVGTGI ERVVATDSRV
CVTAKHSGVV EAVDASRIVI RVDSKKTKAS ELGVDIYNLT KYSRSNQNTC INQKPLVKTG
DKISAADVLA DGPSTDMGEL ALGQNMKIAF MPWNGYNFED SILISEKVIQ EDRYTTIHIE
ELTAYSRDTK LGPEEITADI PNVSELALAK LDEVGVVYVG ARVKGGDILV GKVTPKSETV
LSPEEKLLRA IFGEKANNVK DSSLRVGASK SGVVIDVQIF TRDRVEKDDR ALSIDAERLE
RIKKDIDDEF GIIDGDIFRR VRLKLSGNML SKVAGDIKAG EKLSAKLMKK LDNKDISKLK
VEDAAVNKEV AALIKQAKAK QIEFKKFFEE EKAKINEGAE LPPGVMKMVK VYVATSKTLQ
VGDKMAGRHG NKGVISRVSP VEDMPYLVDG STIDVVLNPL GVPSRMNVGQ VLEVHLGYAA
KGLGYKITAM LDEKRTDMVK QIRDFLDEVY NSYGKQENLA SFSDEEIIEL ASNLREGVPM
ATPVFDGIKE KDIKSLLKLA DLPESGQEQL YDGRTGEPFD RHVTVGYMHM LKLNHLVNDK
MHARSTGPYS LVTQQPLSGK AQFGGQRFGE MEVWALEAYG AAHTLREMLT VKSDDVGGRA
KMYKSIVDGK NLTESIMPES FNVLVKEIRS LGIDVELEQH
