RPOB_HAEDU
ID RPOB_HAEDU Reviewed; 1342 AA.
AC Q7VKL7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=HD_1877;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; AE017143; AAP96608.1; -; Genomic_DNA.
DR RefSeq; WP_010945637.1; NC_002940.2.
DR AlphaFoldDB; Q7VKL7; -.
DR SMR; Q7VKL7; -.
DR STRING; 233412.HD_1877; -.
DR PRIDE; Q7VKL7; -.
DR EnsemblBacteria; AAP96608; AAP96608; HD_1877.
DR KEGG; hdu:HD_1877; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001022; 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 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; 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..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047905"
SQ SEQUENCE 1342 AA; 149853 MW; 4C3666D56CF682DC CRC64;
MAYSYSEKKR IRKSFGKRPQ VLNVPYLLTI QLDSYEKFIH RDLDGQQGLE AAFRSVFPIV
SNNGSTELQY VSYELGEPVF DVRECQIRGT TYAAPLRVKL RLVAFDREAA AGTVKDIKEQ
NVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
GSWLDFEFDP KDNLYARIDR RRKLPATIIL RALGYTTEEI LTMFFEKVLF EIQDNKLLMI
LVPERLRGET AAFDIEANGK IYVERGRRIT ARHIRTLEKD GITQIEVPVE YIVGKVAAKD
YVDLSTGELV CPANTEISMD MLAKLSQAGY KELEVLFTND LDHGPYISET LRVDSTYDRL
SALVEIYRMM RPGEPPTKEA AEALFDNMFF SADRYDLSAV GRMKFNRSLN IPEGVGTGIL
TNDDITGVMK KLIEIRNGRG EVDDIDHLGN RRIRSVGEMA ENQFRIGLVR VERAVRERLS
LGDLDGITPQ DLINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEVTHKRRI SALGPGGLTR
ERAGFEVRDV HPTHYGRLCP IETPEGPNIG LINSLSVYAR TNNYGFLETP FHKVVNGQVT
EEIEYLSAIE EGNYVVAQAN SNLDEHFRFT DTYVTCRGEH GESGLYKPED IHYMDISTQQ
VVSVAAALIP FLEHDDANRA LMGANMQRQA VPTLRADKPL VGTGMEKPIA LDSGVAIVAK
RGGIIQRVDA SRIVVKVNED ETIPGEAGID IYNLIKYTRS NQNTCINQIP CVNLGEPVAR
GEILADGPST DLGELALGQN IRVAFMPWNG YNFEDSMLVS ERVVQEDRFT TIHIQELSCV
ARDTKLGAEE ITADIPNVGE SALSKLDESG IVYVGAEVKG GDILVGKVTP KGETQLTPEE
KLLRAIFGEK ASDVKDSSLR VPNGTSGTVI DVQVFTRDSV EKDKRALEIE EMQLREAKKD
LTEELEILEA GLFTRVRNLL IESGVSEVNL NNVAREKWLE QTLDDEAKQN QLEQLAEQHE
ELCKEFERKL EIKRNKIIQG DDLAPGVLKV VKVYLAVRRQ IQPGDKMAGR HGNKGVISKI
NPVEDMPYDE NGEPVEIVLN PLGVPSRMNI GQILETHLGL AARGIGDQIN AMIKQQQEVT
KLREYIQKAY DLGHGSQVVD LSTFTDEEVM RLAQNLRKGL PLATPVFDGA HEAEIKGLLE
LGGLPTSGQI TLFDGRTGEK FERPVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GTHQMEPGMP
ESFNVLLKEI RALGIDMELD ED
