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AMPR_CITFR
ID   AMPR_CITFR              Reviewed;         291 AA.
AC   P12529;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=HTH-type transcriptional activator AmpR;
GN   Name=ampR;
OS   Citrobacter freundii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2786868; DOI=10.1128/jb.171.7.3746-3753.1989;
RA   Lindquist S., Lindberg F., Normark S.;
RT   "Binding of the Citrobacter freundii AmpR regulator to a single DNA site
RT   provides both autoregulation and activation of the inducible ampC beta-
RT   lactamase gene.";
RL   J. Bacteriol. 171:3746-3753(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16, AND DNA-BINDING.
RX   PubMed=1943705; DOI=10.1111/j.1365-2958.1991.tb01920.x;
RA   Bartowsky E., Normark S.;
RT   "Purification and mutant analysis of Citrobacter freundii AmpR, the
RT   regulator for chromosomal AmpC beta-lactamase.";
RL   Mol. Microbiol. 5:1715-1725(1991).
CC   -!- FUNCTION: Regulates the expression of the beta-lactamase gene.
CC       Represses cephalosporinase (AmpC) in the presence of beta-lactams and
CC       induces it in the absence of them.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; M27222; AAA64510.1; -; Genomic_DNA.
DR   PIR; A32882; A32882.
DR   PDB; 3KOS; X-ray; 1.83 A; A=83-291.
DR   PDB; 3KOT; X-ray; 1.90 A; A=83-291.
DR   PDBsum; 3KOS; -.
DR   PDBsum; 3KOT; -.
DR   AlphaFoldDB; P12529; -.
DR   SMR; P12529; -.
DR   STRING; 1333848.CFNIH1_08420; -.
DR   EvolutionaryTrace; P12529; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   PRINTS; PR00039; HTHLYSR.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW   Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1943705"
FT   CHAIN           2..291
FT                   /note="HTH-type transcriptional activator AmpR"
FT                   /id="PRO_0000105586"
FT   DOMAIN          6..63
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        23..42
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   HELIX           102..107
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   HELIX           109..119
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   STRAND          123..130
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   HELIX           136..139
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   STRAND          142..148
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   STRAND          155..162
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   STRAND          165..169
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   HELIX           171..174
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   HELIX           180..185
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   HELIX           196..203
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   STRAND          215..219
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   HELIX           221..229
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   STRAND          234..238
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   HELIX           243..247
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   STRAND          263..269
FT                   /evidence="ECO:0007829|PDB:3KOS"
FT   HELIX           276..291
FT                   /evidence="ECO:0007829|PDB:3KOS"
SQ   SEQUENCE   291 AA;  32523 MW;  329389631DBA9D2D CRC64;
     MTRSYIPLNS LRAFEAAARH LSFTRAAIEL NVTHSAISQH VKSLEQQLNC QLFVRGSRGL
     MLTTEGESLL PVLNDSFDRM AGMLDRFATK QTQEKLKIGV VGTFAIGCLF PLLSDFKRSY
     PHIDLHISTH NNRVDPAAEG LDYTIRYGGG AWHDTDAQYL CSALMSPLCS PTLASQIQTP
     ADILKFPLLR SYRRDEWALW MQAAGEAPPS PTHNVMVFDS SVTMLEAAQG GMGVAIAPVR
     MFTHLLSSER IVQPFLTQID LGSYWITRLQ SRPETPAMRE FSRWLTGVLH K
 
 
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