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RPOB_BURM1
ID   RPOB_BURM1              Reviewed;        1368 AA.
AC   A9ADI5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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};
GN   OrderedLocusNames=Bmul_0241, BMULJ_03013;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) 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; CP000868; ABX13936.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG44898.1; -; Genomic_DNA.
DR   RefSeq; WP_006400665.1; NC_010804.1.
DR   AlphaFoldDB; A9ADI5; -.
DR   SMR; A9ADI5; -.
DR   STRING; 395019.Bmul_0241; -.
DR   PRIDE; A9ADI5; -.
DR   EnsemblBacteria; BAG44898; BAG44898; BMULJ_03013.
DR   GeneID; 66525168; -.
DR   KEGG; bmj:BMULJ_03013; -.
DR   KEGG; bmu:Bmul_0241; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_4; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000008815; Chromosome 1.
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..1368
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000141671"
SQ   SEQUENCE   1368 AA;  153216 MW;  96E8A7B3CDF8CEA0 CRC64;
     MQYSFTEKKR IRKSFAKRPI VHQVPFLLAT QLESFSTFLQ ADVPATQRKP EGLQAAFTSV
     FPIVSHNGFA RLEFVSYALS APAFNIKECQ QRGLTYCSAL RAKVRLVILD KESPNKPVVK
     EVKEQEVYMG EIPLMTPTGS FVINGTERVI VSQLHRSPGV FFEHDKGKTH SSGKLLFSAR
     IIPYRGSWLD FEFDPKDILY FRVDRRRKMP VTILLKAIGL TPEQILANFF VFDNFTLMDE
     GAQLEFVPER LRGEVARFDI TDRDGKVIVQ KDKRINAKHI RDLEAAKTKF ISVPEDYLLG
     RVLAKNVVDG ETGEVIANAN DEITESVLEK LREAGIKEIQ TLYTNDLDQG PYISSTLRVD
     ETTDKTAARI AIYRMMRPGE PPTEEAVEAL FNRLFYSEEA YDLSKVGRMK FNRRVGRDEI
     TGPMTLQDDD ILATIKILVE LRNGKGEVDD IDHLGNRRVR CVGELAENQF RAGLVRVERA
     VKERLGQAES ENLMPHDLIN SKPISSAIRE FFGSSQLSQF MDQTNPLSEI THKRRVSALG
     PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS LALYAHLNEY GFLETPYRKV
     VDGKVTDQID YLSAIEEGRY MIAQANAAID DEGRLTDELV SSREAGETMM VTPDRIQYMD
     VAPSQIVSVA ASLIPFLEHD DANRALMGSN MQRQAVPCLR PEKPVVGTGI ERTCAVDSGT
     TVQAFRGGVV DYVDAGRIVI RVNDDEAVAG EVGVDIYNLI KYTRSNQNTN INQRPIVKMG
     DKVSRGDVLA DGASTDLGEL ALGQNMLIAF MPWNGYNFED SILISEKVVA DDRYTSIHIE
     ELNVVARDTK LGPEEITRDI SNLAEVQLGR LDESGIVYIG AEVEAGDVLV GKVTPKGETQ
     LTPEEKLLRA IFGEKASDVK DTSLRVPSGM SGTVIDVQVF TREGIQRDKR AQQIIDDELK
     RYRLDLNDQL RIVEGDAFQR LARMLVGKVA NGGPKKLAKG TKIDQAYLED LDHYHWFDIR
     LADDEAAAQL EAIKNSIEEK RHQFDLAFEE KRKKLTQGDE LPPGVLKMVK VYLAVKRRLQ
     PGDKMAGRHG NKGVVSKIVP IEDMPYMADG RPADVVLNPL GVPSRMNVGQ VLEVHLGWAA
     KGLGWRIGEM LQRQAKIEEL RAFLTKIYNE SGRAEDLDSF SDDEILELAK NLREGVPFAT
     PVFDGATEDE MAKMLDLAFP DDIAKQLDMN PSKNQVRLYD GRTGEPFERR VTVGYMHYLK
     LHHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAS YVLQEMLTVK
     SDDVTGRTKV YENLVKGDHV IDAGMPESFN VLVKEIRSLG IDIDLDRN
 
 
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