RPOB_HAEIG
ID RPOB_HAEIG Reviewed; 1343 AA.
AC A5UH20;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
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=CGSHiGG_05825;
OS Haemophilus influenzae (strain PittGG).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374931;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittGG;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABR00076.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP000672; ABR00076.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; A5UH20; -.
DR SMR; A5UH20; -.
DR EnsemblBacteria; ABR00076; ABR00076; CGSHiGG_05825.
DR KEGG; hiq:CGSHiGG_05825; -.
DR HOGENOM; CLU_000524_4_0_6; -.
DR Proteomes; UP000001990; 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; Transcription;
KW Transferase.
FT CHAIN 1..1343
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000329179"
SQ SEQUENCE 1343 AA; 149782 MW; 2A746E86F81CF762 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 LRVDPTYDKI
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 DKVDRTKWLE 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
