ID   ADMX_SERPL              Reviewed;         304 AA.
AC   P0DV33;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   03-AUG-2022, entry version 3.
DE   RecName: Full=HTH-type transcriptional regulator AdmX {ECO:0000305};
GN   Name=admX {ECO:0000303|PubMed:26914969};
GN   ORFNames=AWY96_00730 {ECO:0000312|EMBL:KYQ97099.1};
OS   Serratia plymuthica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=82996;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A153;
RX   PubMed=27198016; DOI=10.1128/genomea.00373-16;
RA   Matilla M.A., Drew A., Udaondo Z., Krell T., Salmond G.P.;
RT   "Genome sequence of Serratia plymuthica A153, a model rhizobacterium for
RT   the investigation of the synthesis and regulation of haterumalides,
RT   zeamine, and andrimid.";
RL   Genome Announc. 4:e00373-e00373(2016).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=A153;
RX   PubMed=26914969; DOI=10.1111/1462-2920.13241;
RA   Matilla M.A., Nogellova V., Morel B., Krell T., Salmond G.P.;
RT   "Biosynthesis of the acetyl-CoA carboxylase-inhibiting antibiotic, andrimid
RT   in Serratia is regulated by Hfq and the LysR-type transcriptional
RT   regulator, AdmX.";
RL   Environ. Microbiol. 18:3635-3650(2016).
RN   [3]
RP   FUNCTION, DNA-BINDING, AND ACTIVITY REGULATION.
RC   STRAIN=A153;
RX   PubMed=30500953; DOI=10.1093/nar/gky766;
RA   Matilla M.A., Daddaoua A., Chini A., Morel B., Krell T.;
RT   "An auxin controls bacterial antibiotics production.";
RL   Nucleic Acids Res. 46:11229-11238(2018).
CC   -!- FUNCTION: Positively regulates the biosynthesis of andrimid, a broad-
CC       spectrum antibiotic, by activating the expression of the adm
CC       biosynthetic gene cluster (PubMed:26914969, PubMed:30500953). It
CC       specifically binds to a region within the adm promoter
CC       (PubMed:30500953). {ECO:0000269|PubMed:26914969,
CC       ECO:0000269|PubMed:30500953}.
CC   -!- ACTIVITY REGULATION: AdmX-mediated transcription is inhibited by
CC       indole-3-acetic and indole-3-pyruvic acids (PubMed:30500953). AdmX
CC       recognizes and binds the auxin indole-3-acetic acid (IAA), which causes
CC       conformational changes in AdmX that result in the inhibition of the
CC       expression of the andrimid gene cluster and the suppression of
CC       antibiotic production (PubMed:30500953). It also recognizes indole-3-
CC       pyruvic acid (IPA), an intermediate of the main IAA biosynthetic
CC       pathway in plants and plant beneficial bacteria, which also prevents
CC       andrimid synthesis, but to a much lesser extent (PubMed:30500953).
CC       {ECO:0000269|PubMed:30500953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Expressed in late logarithmic phase of growth.
CC       {ECO:0000269|PubMed:26914969}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant does not inhibit growth of
CC       B.subtilis and shows decreased adm transcript levels.
CC       {ECO:0000269|PubMed:26914969}.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; LRQU01000001; KYQ97099.1; -; Genomic_DNA.
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   Activator; Cytoplasm; DNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..304
FT                   /note="HTH-type transcriptional regulator AdmX"
FT                   /id="PRO_0000454763"
FT   DOMAIN          1..58
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        18..37
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
SQ   SEQUENCE   304 AA;  34115 MW;  8BEAADC2C52A8032 CRC64;
     MKLRHLEIFY TVMTCGSLSR AAESLNISQP AASKSLKNAE LKLGFKLFQR VRGKLLPSRE
     ALELFEKAQG IYQDLSNLRL LADNLARDPR AKFTLGCLPC LGLSLVPEIA TDFYQQNSNL
     VMTLTAEHTE TLVKKLDLRE IDLALTMQPV QQGDIMATLI AEVPLVYVDK DYRQGAVEID
     SIDQQRWISP GLDSLSTAIA AHRVFPATGL NVETCYMAME FVKRGVGCCI TDIFSARHSL
     TPEMIHQISP PMKIDLYLLR RADASLSPVT QKFVDFLCKR LRNELREINL ELYPGNKKSI
     VSPV