ID   RPOB_HAEIE              Reviewed;        1343 AA.
AC   A5U9X8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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};
GN   OrderedLocusNames=CGSHiEE_00425;
OS   Haemophilus influenzae (strain PittEE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittEE;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(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; CP000671; ABQ97579.1; -; Genomic_DNA.
DR   RefSeq; WP_011961657.1; NC_009566.1.
DR   AlphaFoldDB; A5U9X8; -.
DR   SMR; A5U9X8; -.
DR   KEGG; hip:CGSHiEE_00425; -.
DR   HOGENOM; CLU_000524_4_0_6; -.
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; 2.40.270.10; -; 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; 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..1343
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000051970"
SQ   SEQUENCE   1343 AA;  149804 MW;  DC0637D8DBABB30D CRC64;
     MGYSYSEKKR IRKDFGKRPQ VLNVPYLLTI QLDSFDKFIQ KDPEGQQGLE AAFRSVFPIV
     SNNGYTELQY VDYRLEEPEF DVRECQIRGS TYAAGLRVKL RLVSYDKESS SRAVKDIKEN
     EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
     GSWLDFEFDP KDNLFARIDR RRKLPATIIL RALGYTTEEI LNLFFDKITF EISGDKLLMT
     LVPERLRGET ASFDIEANGK VYVERGRRIT ARHIKALEKD NISQVVVPSE YILGKVASKD
     YVDLESGEII CPANGEISLE TLAKLAQAGY TTIETLFTND LDYGPYISET LRVDPTYDKT
     SALYEIYRMM RPGEPPTPES SEALFNNLFF SAERYDLSTV GRMKFNRSLA FPEGEGAGIL
     SNEDIIAVMR KLIDIRNGRG EVDDIDHLGN RRIRSVGEMA ENQFRIGLVR VERAVKERLS
     LGDLDAITPQ DLINPKPISA AVKEFFGSSQ LSQFMDQNNP LSEVTHKRRI SALGPGGLTR
     ERAGFEVRDV HNTHYGRLCP IETPEGPNIG LINSLSAFAR TNDYGFLETP YRKVVDGQVT
     EEIEYLSAID EANYIIAQAN SNLDENNRFT DAFVTARGER GESGLYKPED IHYMDVSTQQ
     VVSVAAALIP FLEHDDANRA LMGANMQRQA VPTLRADKPL VGTGMEKPIA LDSGVAVVAK
     RGGTVQYVDA SRIVIKVNED ETIAGEAGID IYNLIKYTRS NQNTCINQIP CVNLGDPINR
     GEVLADGPST DLGELALGQN IRVAFMPWNG YNFEDSMLVS ERVVQQDRFT TIHIQELSCV
     ARDTKLGSEE ITADIPNVGE SALSKLDESG IVYVGAEVKG GDILVGKVTP KGETQLTPEE
     KLLRAIFGEK ASDVKDSSLR VPNGTSGTVI DVQVFTRDGV EKDKRALEIE EMQLREAKKD
     LTEELEILEA GLFARVRNLL ISSGADAAQL DKLDRTKWLE QTIADEEKQN QLEQLAEQYE
     ELRKEFEHKL EVKRKKIIKG DDLAPGVLKV VKVYLAVKRQ IQPGDKMAGR HGNKGVISKI
     NPVEDMPYDE NGQPVEIVLN PLGVPSRMNI GQILETHLGL AAKGIGDQIN TMLKQKQEVE
     KLRSYIQKAY DLLGNGSQKV DLSTFTDEEV LRLAGNLRKG LPVATPVFDG ADEAEIKELL
     KLGGLPTSGQ ITLYDGRTGE KFERPVTVGY MYMLKLNHLV DDKMHARSTG SYSLVTQQPL
     GGKAQFGGQR FGEMEVWALE AYGAAYTLQE MLTVKSDDVN GRTKMYKNIV SGNQHMDPGT
     PESFNVIMKE IRSLGLNIEL DEE