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RPOB_SOLUE
ID   RPOB_SOLUE              Reviewed;        1432 AA.
AC   Q01VB1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
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=Acid_5457;
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteria; Bryobacterales; Solibacteraceae;
OC   Candidatus Solibacter.
OX   NCBI_TaxID=234267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin6076;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ86404.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000473; ABJ86404.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041858269.1; NC_008536.1.
DR   AlphaFoldDB; Q01VB1; -.
DR   SMR; Q01VB1; -.
DR   STRING; 234267.Acid_5457; -.
DR   PRIDE; Q01VB1; -.
DR   EnsemblBacteria; ABJ86404; ABJ86404; Acid_5457.
DR   KEGG; sus:Acid_5457; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_0; -.
DR   OrthoDB; 9601at2; -.
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; -; 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; 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; Transcription;
KW   Transferase.
FT   CHAIN           1..1432
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300406"
SQ   SEQUENCE   1432 AA;  160437 MW;  B72D872CDB01E335 CRC64;
     MDLQNYGAAP ERVDFSKIKT SIPIPNLIEV QKKSYERFLQ MDLLPNERED IGLQTVFNSV
     FPISDFRGVS DLEFVDYSIG NWECKCGNLK GLHHLRSTCR NCGATIRTDP FHAGDILCHH
     CGTFNKNVVT FCNKCGDPVG LQLKYDMQEC QERGMTYAAP LKVTIRLTVY SKDPETQKKS
     VRDIKEQEVF FGEIPLMTDN GTFIINGTER VIVSQLHRSP GVFFERVPAQ GYFLGKIIPY
     RGSWVEFEYD NKNILYVRID RKRKFYGSVF LRALGLKTDE QILRAFYRVS KMEIRDKKIY
     WNVDEGLTGL KLSHAITTKS GDTVVGQGKK ITASLFKELQ KAKIEKVEVA PNDLEGAHVV
     ADVVDMTTGE VMIDANSELT TTVMSKLIEA GITEFEIFFP ERDDVGTVIA ATIRKDAVKT
     QNEALIEIYR KLRPGDPPTL DTATQLFQGM FFDPRKYDFS RVGRMKFNIK LYDRSDATAL
     DKRTLDSDDF KSTIRYLLKL RKGIGAVDDI DHLGNRRVRA VGELLENQFR IGLVRMERAI
     KEKMSVYQEM STAMPHDLVN AKPVMAAIRE FFGSSQLSQF MDQTNPLSEI THKRRLSALG
     PGGLSRERAG FEVRDVHPTH YGRICPIETP EGPNIGLISS LSCFARINEY GFIESPYRKV
     IKGAVVDEVK VLNPGDTDYK VGDIVRRGDM DEANRKLGGK KQAAEFEAHC EYLSAWEEDK
     WTIAQANVEL DEKGRIVPDL SNARQAGNFV LKPKEEIEYI DVSPKQLVSV AASLIPFLEN
     DDANRALMGS NMQRQAVPLL RADAPYVGTG MEMVTARDSG AVVLNKRAGV VDSVDSERII
     VRVEGAAHEG QLSREVGADI YQLTKFKRSN QNTCINQKPI VRVGQRVPKG AVLADGPCTD
     LGELALGRNV LVAFMPWRGY NFEDAILVSE KLVKEDYYTS IHIEEFEIEA RDTKLGPEEI
     TRDIPNIADS FLRNLDESGI IRIGATVKPG DILVGKVTPK GETQLTPEEK LLRAIFGEKA
     GDVKDASLYC PPGIEGTIVD CKIFSRKGQE KDERSKAIEE SQIQRLQRNL QDEIRILTDE
     RAKRLGTLLD GKKLLADLHD EKTNKRLLSK DTELTRELIE KMKSRDLKRM RLANKDPRLN
     EQIDEIEEMT SRQIAVLEKI TDEKIAKLRK GDELPPGVIK LVKVYIAMKR KLSVGDKMAG
     RHGNKGVIAR ILPEEDMPYL PDGTPVEIVL NPLGVPSRMN VGQILETHLG WAAKALGVQF
     ATPVFDGATE REIKKNLTAA GLPTSGKTAL FDGMTGTQFE QPVTVGYIYM LKLSHLVDDK
     IHARSIGPYS LITQQPLGGK AQFGGQRFGE MEVWALEAYG AAYILQELLT AKSDDVYGRA
     KIYEAIVKGE AAIEPGVPES FNVLIRELQS LCLDVELMKK PREVPDTALA AD
 
 
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