RPOB_LEGPN
ID RPOB_LEGPN Reviewed; 1368 AA.
AC O86094;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
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};
OS Legionella pneumophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=446;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS RIFAMPICIN RESISTANT.
RC STRAIN=K69, and K91;
RX PubMed=10991843; DOI=10.1128/aac.44.10.2679-2683.2000;
RA Nielsen K., Hindersson P., Hoeiby N., Bangsborg J.M.;
RT "Sequencing of the rpoB gene in Legionella pneumophila and characterization
RT of mutations associated with rifampin resistance in the Legionellaceae.";
RL Antimicrob. Agents Chemother. 44:2679-2683(2000).
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; AF087812; AAC69338.1; -; Genomic_DNA.
DR EMBL; AF101273; AAC95361.1; -; Genomic_DNA.
DR RefSeq; WP_011945543.1; NZ_UGOL01000001.1.
DR AlphaFoldDB; O86094; -.
DR SMR; O86094; -.
DR STRING; 91892.BIZ52_01895; -.
DR PRIDE; O86094; -.
DR eggNOG; COG0085; Bacteria.
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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 Antibiotic resistance; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Transcription; Transferase.
FT CHAIN 1..1368
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047909"
FT VARIANT 537
FT /note="S -> P (in strain: K69 / isolate 8844 and K91 /
FT isolate 8756; rifampicin resistant)"
FT VARIANT 541
FT /note="H -> Y (in strain: K69 / isolate 8751, K69 / isolate
FT 8752, K69 / isolate 8840-43 and K69 / isolate 8845-49;
FT rifampicin resistant)"
FT VARIANT 544
FT /note="R -> H (in strain: K91 / isolate 8755; rifampicin
FT resistant)"
SQ SEQUENCE 1368 AA; 152752 MW; 2381BD26A2C08968 CRC64;
MAVAEAKPQY SHAEKKRFRK SFGKQTDIMP IPNLLEIQLK SYRDFLQTDT KLSEQLNTGL
HAAFSSVFPI ESFSGNARLE YVGYKLGEPA FDVRECKLRG LTYSAPLRVK IRLVVLDKDA
SDDPKPIKDI REQDVFMGEI PLMTDVGTFV VNGTERVVVS QLHRSPGVIF EHDKGKTHSS
GKLLYSARII PYRGSWLDFE FDPKDCVYVR IDRRRKLPVT ILLRALGYEA EDILSEFFET
TRCHLKNGEY HIDLIPQRLR GEIASFDIHV PETGELIVEQ GRRITARHIK QMEKSQMQDL
VVPRDYLIGK TLAKNIIDTS TGEFLAQAND EITEELLDAM ANHGILQIDM IYTNDLDHGS
YISDTLKIDP TGSQLEALVE IYRMMRPGEP PTKEAAEALF KNLFFVEERY DLSAVGRMKF
NRRVGIKSDE GPGTLTKEDI LSVIKTLIDI RNGIGMVDDI DHLGNRRVRS VGEMTENQFR
VGLVRVERAV KERLSLVESE NLMPQDLINA KPVSAAIKEF FGSSQLSQFM DQVNPLSGVT
HKRRVSALGP GGLTRERAGF EVRDVHTTHY GRVCPIETPE GPNIGLINSL SVYARTNEYG
FIETPCRKVV NGRVTDEVEY LSAIEEVDQY IAQSNVELDA QGNILADLVP CRHQNEFSLT
TPDKINYMDV SPKQIVSVAA SLIPFLEHDD ANRALMGSNM QRQAVPTLRS EKPLVGTGME
RIVASDSGVS VVAKRGGVID LVDASRIVVR VNDDETTAGE TGVDIYNLTK YFRSNQDTCI
NQRPIVSTGD RIQRGDVLAD GPCTDMGELA LGQNLLVAFM PWNGYNFEDS ILISERIVHD
DRFTTIHIEE LTCIARDTKL GTEEITADIP NVGESALSNL DESGVVYIGA EVKAGDILVG
KVTPKGETQL TPEEKLLRAI FGEKASDVKD SSLRVPSGMN GTVIDVQVFT RDGLEKDARA
KSIEEEHLAR VRKDLIDERR IREEDIYHRV SHLLLDKVAT GGPGSLKPGS KITQDYLDKV
EREKWFDIRI EDDAVSQQLE QLSKQLELLT KEMEKRFNDS RKKIIQGDDL APGVLKIVKV
YLAVKRRIQP GDKMAGRHGN KGVISIVVPV EDMPHMEDGT AVDIVLNPLG VPSRMNIGQV
LETHLGLAAK GLGRKIAQML DERQTPEAIK AYLEKIYNHD GVQRVNLKCL NDDELMTLAD
NLRAGVPMAT PVFDGATEQE IKSMLQLADL PADGKTVLID GRTGNKFDNP VTVGYMYMLK
LNHLVDDKMH ARSTGSYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAA YTLQEMLTVK
SDDVGGRTKI YKNIVDGDHR MDPGMPESFN VLLKEIRALG IDIELEHD
