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RPOB_NITSB
ID   RPOB_NITSB              Reviewed;        1386 AA.
AC   A6Q1M3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=NIS_0268;
OS   Nitratiruptor sp. (strain SB155-2).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC   Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX   NCBI_TaxID=387092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB155-2;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF69382.1; -; Genomic_DNA.
DR   RefSeq; WP_012081645.1; NC_009662.1.
DR   AlphaFoldDB; A6Q1M3; -.
DR   SMR; A6Q1M3; -.
DR   STRING; 387092.NIS_0268; -.
DR   EnsemblBacteria; BAF69382; BAF69382; NIS_0268.
DR   KEGG; nis:NIS_0268; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_7; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000001118; 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; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 2.
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..1386
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000329184"
SQ   SEQUENCE   1386 AA;  157341 MW;  FD40595E21C5E82B CRC64;
     MLNSLQSGSR LRVDFSKIPQ ELDVPNLLQL QKSSYENFLM ADSKSRENSG IEKVFRSVFP
     IHDPHNRISL EYAGSEIIKP KYTVRECMER GITYSVSLKM NIRLILWERD EKSGEKTGVK
     DVKEQSIYVR DIPYMTDRTS FIINGVERVV VNQLHRSPGV IFKEEEASTS SGTMIHTAQI
     IPDRGAWLYF EYDPKDILYV RINKRRKIPS TILFRALGYS KLDILKLFYP ITKIIIKENK
     FFIEFRPEDF IGRVEFDVRD ENGNLIVEAG KRLTKKKAQK LIEEGVKYIE FPLDVLMDRH
     LASPIIDQES GEVLYDTLTQ LDEHKLKKIL ELGIDEFEIV NDIASGKDRA IINSFIADQE
     SLKLLKQTEG IEDENDLAAI RIYKVMRPGE PVTKETAKAF IQQLFFDPER YDITRVGRMK
     MNHKLGLDVP EYVTVLTSED IIKTVQYLIK VKNGQGHIDD RDHLGNRRIR AIGELLANEL
     HSGLVKMQKA IRDKMSTISG SLDELMPHDL INSKMITNTI LEFFATGQLS QFMDQTNPLS
     EITHKRRLSA LGEGGLVKER AGFEVRDVHP THYGRICPIE TPEGQNIGLI NTLSTYAKVN
     ELGFIEAAYK VVKDGKITDE IVYLTAAQEE GKIIAPANTE IIDGNEIKGD YVEARKDGEI
     ILVEKNKVEL IDLTPRMVVG VAASLIPFLE HDDANRALMG SNMQRQAVPL LRTEAPIVGT
     GMEKVVARDA WESIRARRSG VVEKIDSENI YILGEDENGA YIDHYRLQKN LRTNQNTCFT
     QKPIVKKGQF VEAGQVITDG PNMDHAELAL GKNMLVAFMP WNGYNFEDAI VVSERILRDD
     EFTSVHIYEK EIEARELKHG VEEITRDIPN VKEEEIEHLD ESGIVKIGTY VKPGMILVGK
     VSPKGEVRPS PEERLLRAIF GEKAGHVVNK SLYCPQSMEG VVVDVKIFTK KGYDKDPRAI
     KAYEEEKERL SKEHHDKLLM IDREEMLKII SLLSKEPLEK DAKIKDKEFK AGEKISKEEL
     SQINRFALNA LVKSYAPEVQ KKYNAIKTHF QNEKRKLTEE HEEKLAILEK EDILPSGVVK
     LVKVFIATKR KLKVGDKMAG RHGNKGIVSV IVPEIDMPYT KDGRIVDIVL NPLGVPSRMN
     IGQILEVHLG LIGKKLGEQI QEIFEAKRAD FVKELRQKMI EIADVAKLMN AKETIEKMSD
     EELIEYARDW SKGVKFATPV FEGVTAEEFE KLYELAKMDL DGKTELYDGR TGEKFKERVT
     VGYMYMLKLH HLVDEKVHAR STGPYSLVTQ QPVGGKALFG GQRFGEMEVW ALEAHGAAHT
     LKEMLTIKSD DVEGRVAAYK AITKGEPIPQ PGIPETLFVL TKELQSLGID VEILDEVKDD
     EETGTN
 
 
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