DSPA_SYNY3
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 25-MAY-2022, entry version 152.
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; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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; 1148.1651759; -.
DR PaxDb; P20169; -.
DR EnsemblBacteria; BAA16687; BAA16687; BAA16687.
DR KEGG; syn:sll0698; -.
DR eggNOG; COG5002; Bacteria.
DR InParanoid; P20169; -.
DR OMA; LTFWAVN; -.
DR PhylomeDB; P20169; -.
DR BRENDA; 2.7.13.3; 382.
DR Proteomes; UP000001425; Chromosome.
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: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 transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 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 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; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 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
