位置:首页 > 蛋白库 > RPOB_PSEAE
RPOB_PSEAE
ID   RPOB_PSEAE              Reviewed;        1357 AA.
AC   Q51561;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 132.
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=PA4270;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 480-760.
RA   Yee Y.C., Jin D.J., Yu V.L.;
RT   "A mechanism of resistance of rifampin in Pseudomonas aeruginosa.";
RL   Submitted (DEC-1992) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004091; AAG07658.1; -; Genomic_DNA.
DR   EMBL; M99386; AAA25985.1; -; Genomic_DNA.
DR   PIR; H83112; H83112.
DR   RefSeq; NP_252960.1; NC_002516.2.
DR   RefSeq; WP_003114335.1; NZ_QZGE01000028.1.
DR   AlphaFoldDB; Q51561; -.
DR   SMR; Q51561; -.
DR   STRING; 287.DR97_3641; -.
DR   PaxDb; Q51561; -.
DR   PRIDE; Q51561; -.
DR   EnsemblBacteria; AAG07658; AAG07658; PA4270.
DR   GeneID; 881699; -.
DR   KEGG; pae:PA4270; -.
DR   PATRIC; fig|208964.12.peg.4471; -.
DR   PseudoCAP; PA4270; -.
DR   HOGENOM; CLU_000524_4_0_6; -.
DR   InParanoid; Q51561; -.
DR   OMA; FMTWEGY; -.
DR   PhylomeDB; Q51561; -.
DR   BioCyc; PAER208964:G1FZ6-4343-MON; -.
DR   Proteomes; UP000002438; 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..1357
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047940"
FT   CONFLICT        480
FT                   /note="V -> G (in Ref. 2; AAA25985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        507
FT                   /note="I -> D (in Ref. 2; AAA25985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        585..586
FT                   /note="RT -> AP (in Ref. 2; AAA25985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        655..656
FT                   /note="VT -> AD (in Ref. 2; AAA25985)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1357 AA;  150838 MW;  F6B18383A7EFE4CA CRC64;
     MAYSYTEKKR IRKDFSKLPD VMDVPYLLAI QLDSYREFLQ AGATKEQFRD VGLHAAFKSV
     FPIISYSGNA ALEYVGYRLG EPAFDVKECV LRGVTFAVPL RVKVRLIIFD RESSNKAIKD
     IKEQEVYMGE IPLMTENGTF IINGTERVIV SQLHRSPGVF FDHDRGKTHS SGKLLYSARI
     IPYRGSWLDF EFDPKDCVFV RIDRRRKLPA SVLLRALGYS TEEILNAFYA TNVFHIKGET
     LNLELVPQRL RGEVASIDIK DGSGKVIVEQ GRRITARHIN QLEKAGVSQL EVPFDYLIGR
     TIAKAIVHPA TGEIIAECNT ELTLDLLAKV AKAQVVRIET LYTNDIDCGP FISDTLKIDN
     TSNQLEALVE IYRMMRPGEP PTKEAAETLF GNLFFSAERY DLSAVGRMKF NRRIGRTEIE
     GPGVLSKEDI IDVLKTLVDI RNGKGIVDDI DHLGNRRVRC VGEMAENQFR VGLVRVERAV
     KERLSMAESE GLMPQDLINA KPVAAAIKEF FGSSQLSQFM DQNNPLSEIT HKRRVSALGP
     GGLTRERAGF EVRDVHPTHY GRVCPIETPE GPNIGLINSL ATYARTNKYG FLESPYRVVK
     DSLVTDEIVF LSAIEEADHV IAQASATLNE KGQLVDELVA VRHLNEFTVK APEDVTLMDV
     SPKQVVSVAA SLIPFLEHDD ANRALMGSNM QRQAVPTLRA DKPLVGTGME RNVARDSGVC
     VVARRGGVID SVDASRVVVR VADDEVETGE AGVDIYNLTK YTRSNQNTCI NQRPLVSKGD
     VVARGDILAD GPSTDMGELA LGQNMRVAFM PWNGFNFEDS ICLSERVVQE DRFTTIHIQE
     LTCVARDTKL GPEEITADIP NVGEAALNKL DEAGIVYVGA EVQAGDILVG KVTPKGETQL
     TPEEKLLRAI FGEKASDVKD TSLRVPTGTK GTVIDVQVFT RDGVERDSRA LSIEKMQLDQ
     IRKDLNEEFR IVEGATFERL RAALVGAKAE GGPALKKGTE ITDDYLDGLE RGQWFKLRMA
     DDALNEQLEK AQAYISDRRQ LLDDKFEDKK RKLQQGDDLA PGVLKIVKVY LAIKRRIQPG
     DKMAGRHGNK GVVSVIMPVE DMPHDANGTP VDIVLNPLGV PSRMNVGQIL ETHLGLAAKG
     LGEKINRMLE EQRKVAELRK FLHEIYNEIG GREENLDELG DNEILALAKN LRGGVPMATP
     VFDGAKEREI KAMLKLADLP ESGQMRLFDG RTGNQFERPT TVGYMYMLKL NHLVDDKMHA
     RSTGSYSLVT QQPLGGKAQF GGQRFGEMEV WALEAYGAAY TLQEMLTVKS DDVNGRTKMY
     KNIVDGDHRM EAGMPESFNV LIKEIRSLGI DIELETE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024