ID   AMPR_RHOCA              Reviewed;         289 AA.
AC   P14145;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=HTH-type transcriptional activator AmpR;
GN   Name=ampR;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SP108;
RX   PubMed=2788410; DOI=10.1042/bj2600803;
RA   Campbell J.I.A., Scahill S., Gibson T., Ambler R.P.;
RT   "The phototrophic bacterium Rhodopseudomonas capsulata sp108 encodes an
RT   indigenous class A beta-lactamase.";
RL   Biochem. J. 260:803-812(1989).
CC   -!- FUNCTION: This protein is a positive regulator of gene expression of
CC       cephalosporinase (AmpC).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X15791; CAA33794.1; -; Genomic_DNA.
DR   PIR; S04648; S04648.
DR   RefSeq; WP_035026280.1; NZ_SWJZ01000009.1.
DR   AlphaFoldDB; P14145; -.
DR   SMR; P14145; -.
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   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   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..289
FT                   /note="HTH-type transcriptional activator AmpR"
FT                   /id="PRO_0000105590"
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"
SQ   SEQUENCE   289 AA;  31472 MW;  ABCAFF5687B89008 CRC64;
     MDRPDLPLNA LRVFEVAMRQ GSFTKAAIEL RVTQAAVSHQ VARLEDLLGT ALFLRTSQGL
     IPTDEGRLLF PVLEHGFDAM SRVLDRLGGR RDIEVLKVGV NTTFAMCWLM PRLEAFRQAH
     PQIDLRISTN NNRVEILREG LDMAIRFGTG GWTGHDAIPL AEAPMAPLCA PGLASRLLHP
     SDLGQVTLLR SYRSAEWPGW FEAAGVPCPP VTGPVFDSSV ALAELATSGA GVALLPISMF
     ESYIAQGRLA QPFGVTVSVG RYYLAWPSDR PATSAMSTFS RWLTGQSAE