ATSR_BURTA
ID ATSR_BURTA Reviewed; 602 AA.
AC Q2T0V9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Sensor histidine kinase AtsR {ECO:0000303|PubMed:29914944};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:Q45614};
DE AltName: Full=Global regulator AtsR {ECO:0000303|PubMed:29914944};
GN Name=atsR {ECO:0000303|PubMed:29914944}; OrderedLocusNames=BTH_I0633;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=29914944; DOI=10.1128/aac.00463-18;
RA Wozniak C.E., Lin Z., Schmidt E.W., Hughes K.T., Liou T.G.;
RT "Thailandamide, a Fatty Acid Synthesis Antibiotic That Is Coexpressed with
RT a Resistant Target Gene.";
RL Antimicrob. Agents Chemother. 62:0-0(2018).
CC -!- FUNCTION: Member of a two-component regulatory system involved in
CC control of gene expression; inhibits synthesis of (at least) the
CC polyketide antibiotic thailandamide. Its two-component partner may be
CC BTH_I0635. {ECO:0000305|PubMed:29914944}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:Q45614};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Increased production of thailandamide. Inhibits
CC growth of Salmonella in an overlay assay.
CC {ECO:0000269|PubMed:29914944}.
CC -!- MISCELLANEOUS: Thailandamide is a polyketide that is toxic to human
CC cell lines but also has antibacterial activity on E.coli, S.typhimurium
CC and S.aureus. It probably acts on acetyl-CoA carboxylase in the fatty
CC acid synthesis pathway, which is rarely found to be an antibiotic
CC target. These data suggest it might be a good starting point for
CC engineering of novel antibiotics. {ECO:0000305|PubMed:29914944}.
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DR EMBL; CP000086; ABC38722.1; -; Genomic_DNA.
DR RefSeq; WP_011401822.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2T0V9; -.
DR SMR; Q2T0V9; -.
DR PRIDE; Q2T0V9; -.
DR EnsemblBacteria; ABC38722; ABC38722; BTH_I0633.
DR KEGG; bte:BTH_I0633; -.
DR HOGENOM; CLU_000445_114_59_4; -.
DR OMA; ANMKTIK; -.
DR OrthoDB; 1755994at2; -.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..602
FT /note="Sensor histidine kinase AtsR"
FT /id="PRO_0000452502"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 242..461
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 484..601
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 245
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 533
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 602 AA; 66575 MW; 9E87338D9961B456 CRC64;
MSRVKWRNEK IIVALGSLWI LGFAAWAFLL FDLLGTSVKE GILEGPREGV FWTAAQYRNS
FSRFERQLIL YATRQDRDFD NVLLQLDSLE ASFGFLERPS EVSAYWLSIP KARDDIAELS
RFMATLRRDV PALGARAGDS RRVLEDVARH WPKVNALANY FRAIEMEQRD FTFHQLKEKR
RAIVMLGGVL GVILGALFLL LFYTIRTRGS LLEQQQAALD AQRKASDRAF EMIAAKNAFL
GMVSHELRTP LQAICGSIEV LLARPQSDAN MKTIKRLQNS AASLEAQVKD LTDYIKLRST
NRSVQSDPVE IAPLLADVLD PLRGRIRDKH LNASLRVEPP DLVVKSDRKL IQQIASNLVE
NSIKYTNSGT IAISAELAGT PSNRTMQIAV RDTGVGIAKN LLSKIFEPFF RVNDPGVRHV
DGIGMGLAVV QELVVALRGH VDVRSVVGEG SEFVVTLPVE LPGSADAPDD DAPPSLQTTH
RDLHALVVDD NENARETLGA MLTALGIRAD LRGTGKEGLR CFGECQHDIV VLDLELPDIS
GFEVAEQIRW ATSPDAAKKT TILGVSAYES AMLKGDHAVF DAFVPKPIHL DTLNGIVSRL
RS
