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ARBG_DICCH
ID   ARBG_DICCH              Reviewed;         283 AA.
AC   P26211;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Beta-glucoside operon antiterminator;
GN   Name=arbG;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1732212; DOI=10.1128/jb.174.3.765-777.1992;
RA   el Hassouni M., Henrissat B., Chippaux M., Barras F.;
RT   "Nucleotide sequences of the arb genes, which control beta-glucoside
RT   utilization in Erwinia chrysanthemi: comparison with the Escherichia coli
RT   bgl operon and evidence for a new beta-glycohydrolase family including
RT   enzymes from eubacteria, archeabacteria, and humans.";
RL   J. Bacteriol. 174:765-777(1992).
CC   -!- FUNCTION: Mediates the positive regulation of the beta-glucoside (arb)
CC       operon by functioning as a transcriptional antiterminator. This is an
CC       RNA-binding protein that recognizes a specific sequence located just
CC       upstream of two termination sites within the operon (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated and inactivated by ArbF (EII-Bgl). The degree of
CC       phosphorylation is dependent on the presence or absence of beta-
CC       glucosides which act as inducers of the operon expression. Addition of
CC       inducer result in the rapid dephosphorylation of ArbG (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transcriptional antiterminator BglG family.
CC       {ECO:0000305}.
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DR   EMBL; M81772; AAA24813.1; -; Genomic_DNA.
DR   PIR; A42603; A42603.
DR   AlphaFoldDB; P26211; -.
DR   SMR; P26211; -.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 2.30.24.10; -; 1.
DR   InterPro; IPR004341; CAT_RNA-bd_dom.
DR   InterPro; IPR036650; CAT_RNA-bd_dom_sf.
DR   InterPro; IPR011608; PRD.
DR   InterPro; IPR036634; PRD_sf.
DR   InterPro; IPR001550; Transcrpt_antitermin_CS.
DR   Pfam; PF03123; CAT_RBD; 1.
DR   Pfam; PF00874; PRD; 2.
DR   SMART; SM01061; CAT_RBD; 1.
DR   SUPFAM; SSF50151; SSF50151; 1.
DR   SUPFAM; SSF63520; SSF63520; 2.
DR   PROSITE; PS00654; PRD_1; 1.
DR   PROSITE; PS51372; PRD_2; 2.
PE   3: Inferred from homology;
KW   Activator; Phosphoprotein; Repeat; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..283
FT                   /note="Beta-glucoside operon antiterminator"
FT                   /id="PRO_0000204243"
FT   DOMAIN          65..170
FT                   /note="PRD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT   DOMAIN          171..280
FT                   /note="PRD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
SQ   SEQUENCE   283 AA;  32820 MW;  A589ADBDF011A648 CRC64;
     MKIAKILNNN VVTVMDEQNN EQVVMGRGLG FKKRPGDTVN AALIEKIFSL RSSELTARLS
     DVLERIPLEV VTTADRIIAL AKEKLGGNLQ NSLYISLTDH CHFAIERHRQ GVDIRNGLQW
     EVKRLYQKEF AIGLDALDII HRRLGVRLPE DEAGFIALHL VNAQLDSHMP EVMRITRVMQ
     EILNIVKYQL NLDYNEQAFS YHRFVTHLKF FAQRLLGRTP VFSEDESLHD VVKEKYTLAY
     HCAEKIQDHI MLHYDYTLTK EELMFLAIHI ERVRSELQEQ TAE
 
 
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