ID   RPOB_RUEPO              Reviewed;        1378 AA.
AC   Q5LMQ5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=SPO3508;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV96733.1; -; Genomic_DNA.
DR   RefSeq; WP_011049188.1; NC_003911.12.
DR   AlphaFoldDB; Q5LMQ5; -.
DR   SMR; Q5LMQ5; -.
DR   STRING; 246200.SPO3508; -.
DR   PRIDE; Q5LMQ5; -.
DR   EnsemblBacteria; AAV96733; AAV96733; SPO3508.
DR   KEGG; sil:SPO3508; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_5; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000001023; 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; 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..1378
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224108"
SQ   SEQUENCE   1378 AA;  153272 MW;  B4E2303E87B3A062 CRC64;
     MAQTFLGQKR LRKYYGKIRE VLEMPNLIEV QKSSYDLFLN SGDAPQPLDG EGIMGVFQSV
     FPIKDFNETS VLEFVKYELE KPKYDVEECM QRDMTYSAPL KVTLRLIVFD VDEDTGAKSV
     KDIKEQDVFM GDMPLMTPNG TFIVNGTERV IVSQMHRSPG VFFDHDKGKT HSSGKLLFAC
     RIIPYRGSWL DFEFDAKDIV FARIDRRRKL PVTTLLYALG LDQEGIMDAY FKTVSYRLEK
     KRGWVTPFFP ERVRGTRPTY DLIDAASGEV IAEAGKKVTP RAVKKLIEEG SVTDLLVPFD
     HIVGKFAAKD IINEETGAIY VEAGDELTLE YDKDGDLIGG TVKELIDNGV TNIPVLDIDN
     INVGPYIRNT MAQDKNMNRE TALMDIYRVM RPGEPPTVEA ASALFDTLFF DSERYDLSAV
     GRVKMNMRLD LDAADTQRTL RREDIIACIK ALVELRDGKG DIDDIDHLGN RRVRSVGELM
     ENQYRVGLLR MERAIKERMS SVEIDTVMPQ DLINAKPAAA AVREFFGSSQ LSQFMDQTNP
     LSEVTHKRRL SALGPGGLTR ERAGFEVRDV HPTHYGRMCP IETPEGPNIG LINSLATFAR
     VNKYGFIETP YRVVKGGQVT DEVHYMSATE EMRHTVAQAN ATLDENGKFV NELVNTRQAG
     DYTLAPMESV DLIDVSPKQL VSVAASLIPF LENDDANRAL MGSNMQRQAV PLLRAEAPLV
     GTGIEEKVAI DSGAAIQAKR AGIIDQIDAQ RIVIRATEDL ELGDAGVDIY RMRKFQRSNQ
     NTCINQRPLV KVGQQVSKGE VIADGPSTDM GELALGKNVV VAFMPWNGYN YEDSILISER
     IARDDVFTSI HIEEFEVAAR DTKLGPEEIT RDIPNVGEEA LRNLDEAGIV YIGAEVQPGD
     ILVGKITPKG ESPMTPEEKL LRAIFGEKAS DVRDTSLRVK PGDYGTVVEV RVFNRHGVDK
     DERALQIERE EVERLARDRD DELAILDRNI YARLKSLILG KTAVKGPKGI KPGSEITEEL
     LETLTRGQWW MLALEGEQDA QIVEALNEQY ELQKRALDAR FEDKVEKVRR GDDLPPGVMK
     MVKVFIAVKR KLQPGDKMAG RHGNKGVISK VVPMEDMPFL ADGTPVDFCL NPLGVPSRMN
     VGQILETHMG WAARGLGLNV DEALQEYRRS GDLTPVRDAM KHAYGEDVYA EGISGMDEDT
     LVEAAGNVTR GVPIATPVFD GAKEADVNDA LTRAGFDTSG QSVLFDGRTG EQFARPVTVG
     IKYLLKLHHL VDDKIHARST GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL EAYGAAYTLQ
     EMLTVKSDDV AGRTKVYESI VKGEDNFEAG IPESFNVLVK EVRGLGLNME LLDAEVEE