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URER_PROMH
ID   URER_PROMH              Reviewed;         293 AA.
AC   Q02458; B4EXN1;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Urease operon transcriptional activator;
GN   Name=ureR; OrderedLocusNames=PMI3681;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7678244; DOI=10.1128/jb.175.2.465-473.1993;
RA   Nicholson E.B., Concaugh E.A., Foxall P.A., Island M.D., Mobley H.L.T.;
RT   "Proteus mirabilis urease: transcriptional regulation by UreR.";
RL   J. Bacteriol. 175:465-473(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
RN   [3]
RP   UREASE AS A VIRULENCE FACTOR.
RX   PubMed=2180821; DOI=10.1128/iai.58.4.1120-1123.1990;
RA   Jones B.D., Lockatell C.V., Johnson D.E., Warren J.W., Mobley H.L.T.;
RT   "Construction of a urease-negative mutant of Proteus mirabilis: analysis of
RT   virulence in a mouse model of ascending urinary tract infection.";
RL   Infect. Immun. 58:1120-1123(1990).
RN   [4]
RP   MODE OF ACTION, PROBABLE OPERON STRUCTURE, AND MUTAGENESIS OF ASP-180 AND
RP   PRO-222.
RX   PubMed=7559355; DOI=10.1128/jb.177.19.5653-5660.1995;
RA   Island M.D., Mobley H.L.T.;
RT   "Proteus mirabilis urease: operon fusion and linker insertion analysis of
RT   ure gene organization, regulation, and function.";
RL   J. Bacteriol. 177:5653-5660(1995).
CC   -!- FUNCTION: Positive regulator of the expression of the urease operon.
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DR   EMBL; Z18752; CAA79243.1; -; Genomic_DNA.
DR   EMBL; AM942759; CAR47179.1; -; Genomic_DNA.
DR   PIR; A40644; A40644.
DR   RefSeq; WP_012368846.1; NC_010554.1.
DR   AlphaFoldDB; Q02458; -.
DR   SMR; Q02458; -.
DR   STRING; 529507.PMI3681; -.
DR   EnsemblBacteria; CAR47179; CAR47179; PMI3681.
DR   GeneID; 6801578; -.
DR   KEGG; pmr:PMI3681; -.
DR   eggNOG; COG2207; Bacteria.
DR   HOGENOM; CLU_1026225_0_0_6; -.
DR   Proteomes; UP000008319; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR   Pfam; PF12833; HTH_18; 1.
DR   PRINTS; PR00032; HTHARAC.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation; Virulence.
FT   CHAIN           1..293
FT                   /note="Urease operon transcriptional activator"
FT                   /id="PRO_0000194591"
FT   DOMAIN          171..268
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   DNA_BIND        188..209
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   DNA_BIND        235..258
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   MUTAGEN         180
FT                   /note="D->DPSTD: Abrogates activity."
FT                   /evidence="ECO:0000269|PubMed:7559355"
FT   MUTAGEN         222
FT                   /note="P->PIRRR: Abrogates activity."
FT                   /evidence="ECO:0000269|PubMed:7559355"
FT   CONFLICT        221
FT                   /note="M -> I (in Ref. 1; CAA79243)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="P -> G (in Ref. 2; CAR47179)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   293 AA;  33456 MW;  97A8EA21C0A2506A CRC64;
     MEYKHILSSN QISLKTFYIE NPMIAIVYGA KGEICINGQT ITVTTNLTLI IPKYSQVSCD
     VTNFFPTKPI ELHTLVLSET ELQSVFSLLK PLIKSGAPIT RHLPDYHLST PEVVKTNFTL
     LQQCLPLEHG TPSQETLFMQ QSLFFILLAV YHEGVDILNI FRFNYDEPKN QAITHLITQD
     PQRKWHLEDV AKTLYTTPST LRRHLSKEGV SFCQLLLDVR MPIALNYLTF SNYSVFQISH
     RCGFGSNAYF CDAFKRKYGM TPSQFRTQSR QANDPNAIAT MASQNDESIK KVF
 
 
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