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AMPR_PSEAE
ID   AMPR_PSEAE              Reviewed;         296 AA.
AC   P24734;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 3.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=HTH-type transcriptional activator AmpR;
GN   Name=ampR; OrderedLocusNames=PA4109;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=8405939; DOI=10.1111/j.1574-6968.1993.tb06404.x;
RA   Lodge J.M., Busby S.J.W., Piddock L.J.V.;
RT   "Investigation of the Pseudomonas aeruginosa ampR gene and its role at the
RT   chromosomal ampC beta-lactamase promoter.";
RL   FEMS Microbiol. Lett. 111:315-320(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=2125210; DOI=10.1042/bj2720627;
RA   Lodge J.M., Minchin S.D., Piddock L.J.V., Busby S.J.W.;
RT   "Cloning, sequencing and analysis of the structural gene and regulatory
RT   region of the Pseudomonas aeruginosa chromosomal ampC beta-lactamase.";
RL   Biochem. J. 272:627-631(1990).
RN   [4]
RP   SEQUENCE REVISION TO 6.
RA   Lodge J.M.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is a positive regulator of gene expression of
CC       beta-lactamase (AmpC). {ECO:0000269|PubMed:8405939}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; X67095; CAA47470.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG07496.1; -; Genomic_DNA.
DR   EMBL; X54719; CAA38523.2; -; Genomic_DNA.
DR   PIR; E83132; E83132.
DR   PIR; S24954; S24954.
DR   RefSeq; NP_252798.1; NC_002516.2.
DR   RefSeq; WP_003101291.1; NZ_QZGE01000013.1.
DR   PDB; 5MMH; X-ray; 2.20 A; A/B/C/D=84-296.
DR   PDBsum; 5MMH; -.
DR   AlphaFoldDB; P24734; -.
DR   SMR; P24734; -.
DR   STRING; 287.DR97_3762; -.
DR   PaxDb; P24734; -.
DR   PRIDE; P24734; -.
DR   EnsemblBacteria; AAG07496; AAG07496; PA4109.
DR   GeneID; 877983; -.
DR   KEGG; pae:PA4109; -.
DR   PATRIC; fig|208964.12.peg.4305; -.
DR   PseudoCAP; PA4109; -.
DR   HOGENOM; CLU_039613_37_0_6; -.
DR   OMA; TNNNRVD; -.
DR   PhylomeDB; P24734; -.
DR   BioCyc; PAER208964:G1FZ6-4182-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   CollecTF; EXPREG_000009a0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1900232; P:negative regulation of single-species biofilm formation on inanimate substrate; IMP:PseudoCAP.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IMP:PseudoCAP.
DR   GO; GO:0045862; P:positive regulation of proteolysis; IMP:PseudoCAP.
DR   GO; GO:1900378; P:positive regulation of secondary metabolite biosynthetic process; IMP:PseudoCAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:PseudoCAP.
DR   GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR   CDD; cd08484; PBP2_LTTR_beta_lactamase; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR037420; AmpR_PBP2.
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; DNA-binding; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..296
FT                   /note="HTH-type transcriptional activator AmpR"
FT                   /id="PRO_0000105589"
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   CONFLICT        12
FT                   /note="R -> A (in Ref. 1; CAA47470 and 3; CAA38523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="A -> G (in Ref. 1; CAA47470)"
FT                   /evidence="ECO:0000305"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   HELIX           102..107
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   HELIX           109..119
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   HELIX           136..139
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   STRAND          142..148
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   STRAND          155..162
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   STRAND          165..169
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   HELIX           171..175
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   HELIX           180..185
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   HELIX           196..203
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   STRAND          213..220
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   HELIX           221..229
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   STRAND          234..238
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   HELIX           243..247
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   STRAND          263..269
FT                   /evidence="ECO:0007829|PDB:5MMH"
FT   HELIX           276..296
FT                   /evidence="ECO:0007829|PDB:5MMH"
SQ   SEQUENCE   296 AA;  32603 MW;  8092C376D7D91605 CRC64;
     MVRPHLPLNA LRAFEASARH LSFTRAAIEL CVTQAAVSHQ VKSLEERLGV ALFKRLPRGL
     MLTHEGESLL PVLCDSFDRI AGLLERFEGG HYRDVLTVGA VGTFTVGWLL PRLEDFQARH
     PFIDLRLSTH NNRVDIAAEG LDYAIRFGGG AWHGTEALAL FEAPLTVLCC PEVAAQLHSP
     ADLLQHTLLR SYRADEWPLW FQAAGLPAHA PLTRSIVFDT SLAMLEAARQ GVGVALAPAA
     MFARQLASES IRRPFATEVS TGSYWLTRLQ SRGETSAMLA FRGWLLEMAA VEARGR
 
 
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