ID   RPOB_HAEIN              Reviewed;        1343 AA.
AC   P43738;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 132.
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=HI_0515;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22173.1; -; Genomic_DNA.
DR   PIR; H64073; H64073.
DR   RefSeq; NP_438673.1; NC_000907.1.
DR   RefSeq; WP_005666423.1; NC_000907.1.
DR   AlphaFoldDB; P43738; -.
DR   SMR; P43738; -.
DR   STRING; 71421.HI_0515; -.
DR   PRIDE; P43738; -.
DR   EnsemblBacteria; AAC22173; AAC22173; HI_0515.
DR   KEGG; hin:HI_0515; -.
DR   PATRIC; fig|71421.8.peg.534; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_6; -.
DR   OMA; FMTWEGY; -.
DR   PhylomeDB; P43738; -.
DR   BioCyc; HINF71421:G1GJ1-528-MON; -.
DR   Proteomes; UP000000579; 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..1343
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047906"
SQ   SEQUENCE   1343 AA;  149784 MW;  4EF99CD648686A44 CRC64;
     MGYSYSEKKR IRKDFGKRPQ VLNVPYLLTI QLDSFDKFIQ KDPEGQQGLE AAFRSVFPIV
     SNNGYTELQY VDYRLEEPEF DVRECQIRGS TYAAGLRVKL RLVSYDKESS SRAVKDIKEN
     EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
     GSWLDFEFDP KDNLFARIDR RRKLPATIIL RALGYTTEEI LNLFFDKITF EIAGDKLLMT
     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
     EEIEYLSVID EANYIIAQAN SNLDENNRFT DAFVTARGER GESGLYKPED IHYMDVSTQQ
     VVSVAAALIP FLEHDDANRA LMGANMQRQA VPTLRADKPL VGTGMEKPIA LDSGVAVVAK
     RGGTVQYVDA SRIVIKVNED ETIAGEAGID IYNLIKYTRS NQNTCINQIP CVNLGDPINR
     GEVLADGPST DLGELALGQN IRVAFMPWNG YNFEDSMLVS ERVVQQDRFT TIHIQELSCV
     ARDTKLGAEE 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 AMLKQKQEVE
     KLRSYIQKAY DLLGNGSQKV DLSTFTDEEV LRLAGNLRKG LPVATPVFDG ADEAEIKELL
     KLGGLPTSGQ ITLYDGRTGE KFERPVTVGY MYMLKLNHLV DDKMHARSTG SYSLVTQQPL
     GGKAQFGGQR FGEMEVWALE AYGAAYTLQE MLTVKSDDVN GRTKMYKNIV SGNQHMEPGT
     PESFNVIMKE IRSLGLNIEL DEE