RPOB_ACTP2
ID RPOB_ACTP2 Reviewed; 1342 AA.
AC A3N325;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=APL_1727;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN74811.1; -; Genomic_DNA.
DR RefSeq; WP_005613296.1; NC_009053.1.
DR AlphaFoldDB; A3N325; -.
DR SMR; A3N325; -.
DR STRING; 416269.APL_1727; -.
DR PRIDE; A3N325; -.
DR EnsemblBacteria; ABN74811; ABN74811; APL_1727.
DR KEGG; apl:APL_1727; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001432; 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..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300272"
SQ SEQUENCE 1342 AA; 149710 MW; CB204AD9BACE1099 CRC64;
MAYSYSEKKR IRKSFGKRPQ VLNVPYLLTI QLDSYEKFIQ RDSDGQQGLE AAFRSVFPIV
SNNGSTELQY VSYELGEPVF DVRECQIRGT TYAAPLRVKL RLVTFDREAA AGTVKDIKEQ
NVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
GSWLDFEFDP KDNLYARIDR RRKLPATIIL RALGYTTEEI LSMFFDKVNF EIQDNKLLMT
LVPERLRGET AAFDIEANGK VYVERGRRIT ARHIRTLEKD GITQIEVPVE YIVGKVAAKD
YVDLSTGEVV CPANMEISME MLAKLSQAGY KEIEVLFTND LDHGPYISET LRVDPTYDRL
SALVEIYRMM RPGEPPTKEA AEALFDNMFF SADRYDLSAV GRMKFNRSLN LEEGVGSGIL
SNDDITGVMK KLIEIRNGRG EVDDIDHLGN RRIRSVGEMA ENQFRIGLVR VERAVRERLS
LGDLDGITPQ DLINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEVTHKRRI SALGPGGLTR
ERAGFEVRDV HTTHYGRLCP IETPEGPNIG LINSLSVYAR TNNYGFLETP FRKVVNGQVT
EDIEYLSAIE EGNYVIAQAN SNLDENFRFT DTYVTCRGEH GESGLYKPED IHYMDISTQQ
VVSVAAALIP FLEHDDANRA LMGANMQRQA VPTLRADKPL VGTGMEKPIA LDSGVAIVAK
RGGIVQRVDA SRIVVKVNED ETIPGEAGID IYNLIKYTRS NQNTCINQIP CVNLGEPVAR
GEILADGPST DLGELALGQN IRVAFMPWNG YNFEDSMLVS ERVVQEDRFT TIHIQELSCV
ARDTKLGAEE ITADIPNVGE SALSKLDESG IVYVGAEVKG GDILVGKVTP KGETQLTPEE
KLLRAIFGEK ASDVKDSSLR VPNGTSGTVI DVQVFTRDGV EKDKRALEIE EMQLKEAKKD
LTEELEILEA GLFTRVRNLL IEGGVSEAEL DKVAREKWLE QTLDDEAKQN QLEQLAEQHE
ELRKEFERKL EIKRNKIIQG DDLAPGVLKV VKVYLAVRRQ IQPGDKMAGR HGNKGVISKI
NPVEDMPYDE NGQPVEIVLN PLGVPSRMNI GQILETHLGL AAKGIGDQIN AMIKQQQSVA
KLREYIQKAY DLGHGSQSVD LSTFTDEEVM RLAENLRKGL PLATPVFDGA HESEIKGLLE
LGGLPTSGQI TLFDGRTGEK FERPVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GTHQMEPGMP
ESFNVLLKEI RALGIDMELD EE
