(data stored in ACNUC7421 zone)

SWISSPROT: RPOB_LEGPC

ID   RPOB_LEGPC              Reviewed;        1368 AA.
AC   A5IHS1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 75.
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=LPC_3021;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
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}.
DR   EMBL; CP000675; ABQ56921.1; -; Genomic_DNA.
DR   RefSeq; WP_011945543.1; NC_009494.2.
DR   SMR; A5IHS1; -.
DR   PRIDE; A5IHS1; -.
DR   EnsemblBacteria; ABQ56921; ABQ56921; LPC_3021.
DR   KEGG; lpc:LPC_3021; -.
DR   HOGENOM; HOG000218612; -.
DR   KO; K03043; -.
DR   OMA; FMTWEGY; -.
DR   BioCyc; LPNE400673:LPC_RS01880-MONOMER; -.
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; 2.40.270.10; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 1.
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;
DR   PRODOM; A5IHS1.
DR   SWISS-2DPAGE; A5IHS1.
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW   Transferase.
FT   CHAIN           1..1368
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000051971"
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
//

If you have problems or comments...

PBIL Back to PBIL home page