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RPOB_BIFLS
ID   RPOB_BIFLS              Reviewed;        1187 AA.
AC   B7GUG7; E8MMC7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Blon_2049, BLIJ_2127;
OS   Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS   1222 / NCTC 11817 / S12).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=391904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA   Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA   Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA   Richardson P.M., Mills D.A.;
RT   "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT   adaptations for milk utilization within the infant microbiome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=21270894; DOI=10.1038/nature09646;
RA   Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA   Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA   Morita H., Hattori M., Ohno H.;
RT   "Bifidobacteria can protect from enteropathogenic infection through
RT   production of acetate.";
RL   Nature 469:543-547(2011).
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; CP001095; ACJ53113.1; -; Genomic_DNA.
DR   EMBL; AP010889; BAJ69704.1; -; Genomic_DNA.
DR   RefSeq; WP_012578318.1; NZ_JDTT01000005.1.
DR   AlphaFoldDB; B7GUG7; -.
DR   SMR; B7GUG7; -.
DR   PRIDE; B7GUG7; -.
DR   EnsemblBacteria; ACJ53113; ACJ53113; Blon_2049.
DR   KEGG; bln:Blon_2049; -.
DR   KEGG; blon:BLIJ_2127; -.
DR   PATRIC; fig|391904.8.peg.2134; -.
DR   HOGENOM; CLU_000524_4_1_11; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000001360; 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; 1.
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..1187
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000165790"
FT   REGION          1150..1187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1173..1187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1187 AA;  131648 MW;  EF1F39C112D9F526 CRC64;
     MATESTTNTT TIIARADQHD IDLHKASDRV NFGSIKEPID VPYLLGVQTD SFDWLIGSDR
     WKARVEEDEK NGTNTVAHTS GLDEVFNEIS PIENFAQTMS LTFSDPYFEE PRHTVQECKE
     KDYTYSAPLY VNAEFENGDT GEIKSQTVFM GDFPLQTPHG TFIIGGTERV IVSQLVRSPG
     VYFDRQQDRT SDKEVFGAKI IPSRGAWLEF EIDKKDQPQV RVDRKRKQSA IVFLMAIGMT
     KSEIAQAFKD YPLVLDALEK ETLETQDEAL VDLYRKIRPA DTPTPEAGKN LLDSFYFNTK
     RYDLARVGRY KINRKLGVEA DFNDRSLHQE DIIATIKYLV ALHDGAATFP GKRNGEDVDL
     RVDVDDIDHF GNRRIRQVGE LIQNQLRTGL SRMERVVRER MTTQDAEAIT PQSLINIRPV
     NATIKEFFGT SQLSQFMDQN NPLSGVTNKR RLSALGPGGL SRDRASMEVR DVHPSHFGRM
     CPIESPEGPN IGLIGSLATF GRVNPFGFIE TPYRKVVNGH VTDEVEYMTA DRDLDHVIAQ
     ANQELDENGN FVSKSALARV GEEEAVDVPV SSVDYMDVSP RQMVSLGASL IPFLEHDEGH
     RALMGTNMQR QAVPLIESER PLVGTGSEWR AANDSGDVIK SEKDGVVTYV SADLIRVMND
     DGTTSSYKLA KFQRSNQTTC YNQRPIIHDG ERVEAGSVLA DGPAIQKGDL ALGKNLLIAF
     MPWNGYNYED AVIISQRLVQ DDTLSSIHIE EYEIDARETK LGAEEITRDL PNVGEDAVAN
     LDERGIIRIG AEVEAGDILV GKVTPKGETE LTPEERLLRA IFGEKSREVR DTSLRVPHGE
     TGTVIGVKEI TREDAEEDGD ELPNGVNQMI RVYIAQHRKI TVGDKLSGRH GNKGCISRIL
     PEEDMPFLAD GTPVDIMLNP LGVPSRMNLG QVLELHLGWI AHSGWDISLD PNMEAEWKKL
     VPSGAEKAEP NTPVATPVFD GVKPEVLKGL LSTTLPNRDG DRLVGPDGKA TLFDGRTGEP
     YTKPISVGYM YMLKLHHLVD DKIHARSTGP YSMITQQPLG GKAQFGGQRF GEMEVWALEA
     YGAAYTLHEM MTTKSDDVDG RVRVYGAIVK GDNLPPAGIP ESFKVLLKEM QSLSLNVEVL
     NAEGVAIDMK DEDDDPASSA DDLGFNIGAR PDAAAKEDQK AEEPEYQ
 
 
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