ID   DSPA_SYNY3              Reviewed;         663 AA.
AC   P20169; Q55232;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Drug sensory protein A;
DE            EC=2.7.13.3;
GN   Name=dspA; Synonyms=dfr; OrderedLocusNames=sll0698;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8535519; DOI=10.1099/13500872-141-11-2915;
RA   Bartsevich V.V., Shestakov S.V.;
RT   "The dspA gene product of the cyanobacterium Synechocystis sp. strain PCC
RT   6803 influences sensitivity to chemically different growth inhibitors and
RT   has amino acid similarity to histidine protein kinases.";
RL   Microbiology 141:2915-2920(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RX   PubMed=3141423; DOI=10.1016/s0021-9258(19)77887-9;
RA   Reilly P., Hulmes J.D., Pan Y.-C.E., Nelson N.;
RT   "Molecular cloning and sequencing of the psaD gene encoding subunit II of
RT   photosystem I from the cyanobacterium, Synechocystis sp. PCC 6803.";
RL   J. Biol. Chem. 263:17658-17662(1988).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Mutations in dspA results in resistance to herbicides
CC       difunon, diuron and calmodulin antagonists chlorpromazine and
CC       trifluoperazine.
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DR   EMBL; X72856; CAA51377.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA16687.1; -; Genomic_DNA.
DR   EMBL; J04195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S74535; S74535.
DR   AlphaFoldDB; P20169; -.
DR   SMR; P20169; -.
DR   IntAct; P20169; 1.
DR   STRING; 1148.gene:10497542; -.
DR   PaxDb; 1148-1651759; -.
DR   EnsemblBacteria; BAA16687; BAA16687; BAA16687.
DR   KEGG; syn:sll0698; -.
DR   eggNOG; COG5002; Bacteria.
DR   InParanoid; P20169; -.
DR   PhylomeDB; P20169; -.
DR   BRENDA; 2.7.13.3; 382.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF32; DRUG SENSORY PROTEIN A; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Herbicide resistance; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..663
FT                   /note="Drug sensory protein A"
FT                   /id="PRO_0000074758"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          220..272
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          281..351
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          429..656
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         432
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   663 AA;  74536 MW;  42CD7CA67E396586 CRC64;
     MGTSVSNPTA ILQTMQGFLR KWWSEFNLQT RLMAAATLVV SLLMSGLTFW AVNTIQEDAQ
     LVDTRFGRDV GLLLAANVAP MIADKNLTEV ARFSSRFYEN TSNIRYMIYA DPSGKIFFGI
     PYSEETVQNS LTLERRIELP QIDPHNFDQP FVRQHHTPNG DVTDVFIPLQ YQGKFLGVLA
     IGINPNPAAV NSSNLTRDVT IAVFISIWVM VILGAVFNAL TITQPIKELL LGVKNIAAGN
     FKQRITLPFG GELGELIVNF NEMAERLERY EAQNIEELTA EKAKLDTLVS TIADGAMLVD
     TNLQLLLVNP TARRLFAWEN KPIIGENLLE NLPPEITAQL TQPLRELAAD QGSLLFSPGH
     GPQEEEQDKT YAPEEFRISL TQPFPRTIRL MLTQVLDQNR ENLRGIVMTV QDITREVELN
     EAKSQFISNV SHELRTPLFN IKSFIETLSE FGEDLSEVER KEFLETANHE TDRLSRLVND
     VLDLSKLESS KIYQLDAVDL YQLIEQSLRS YQLNAKDKQL QLEKILDPDL PFALGNYDLL
     LQVMTNLIGN SFKFTKAGGK IIVRAYPLHR SNLRAEDGPG LVRVEISDTG IGIDPEDQAA
     IFERFYRVEN RVHTLEGTGL GLSIVKNIIA KHQSQIHLVS EVGVGTTFWF DLAVYQSMLM
     VVG
//