ID G3XD98_PSEAE Unreviewed; 925 AA.
AC G3XD98;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=gacS {ECO:0000313|EMBL:AAG04317.1};
GN OrderedLocusNames=PA0928 {ECO:0000313|EMBL:AAG04317.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG04317.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG04317.1, ECO:0000313|Proteomes:UP000002438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA Hancock R.E., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0007829|PDB:5O7J}
RP STRUCTURE BY NMR OF 38-164.
RX PubMed=28900144; DOI=10.1038/s41598-017-11361-3;
RA Ali-Ahmad A., Fadel F., Sebban-Kreuzer C., Ba M., Pelissier G.D.,
RA Bornet O., Guerlesquin F., Bourne Y., Bordi C., Vincent F.;
RT "Structural and functional insights into the periplasmic detector domain of
RT the GacS histidine kinase controlling biofilm formation in Pseudomonas
RT aeruginosa.";
RL Sci. Rep. 7:11262-11262(2017).
RN [3] {ECO:0007829|PDB:7N0E}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 285-344.
RX PubMed=34529974; DOI=10.1016/j.jbc.2021.101193;
RA Ryan Kaler K.M., Nix J.C., Schubot F.D.;
RT "RetS inhibits Pseudomonas aeruginosa biofilm formation by disrupting the
RT canonical histidine kinase dimerization interface of GacS.";
RL J. Biol. Chem. 297:101193-101193(2021).
RN [4] {ECO:0007829|PDB:7QZ2, ECO:0007829|PDB:7QZO}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 662-793 IN COMPLEX WITH MG(2+).
RX PubMed=35767996; DOI=10.1016/j.str.2022.06.002;
RA Fadel F., Bassim V., Francis V.I., Porter S.L., Botzanowski T., Legrand P.,
RA Perez M.M., Bourne Y., Cianferani S., Vincent F.;
RT "Insights into the atypical autokinase activity of the Pseudomonas
RT aeruginosa GacS histidine kinase and its interaction with RetS.";
RL Structure 30:1285-1297.e5(2022).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AE004091; AAG04317.1; -; Genomic_DNA.
DR PIR; E83529; E83529.
DR RefSeq; NP_249619.1; NC_002516.2.
DR RefSeq; WP_003102426.1; NZ_QZGE01000007.1.
DR PDB; 5O7J; NMR; -; A=38-164.
DR PDB; 7N0E; X-ray; 2.30 A; A=285-344.
DR PDB; 7QZ2; X-ray; 1.87 A; A/B=662-793.
DR PDB; 7QZO; X-ray; 1.45 A; A/B=662-793.
DR PDB; 7Z8N; X-ray; 2.64 A; A/B/C/D=220-512.
DR PDBsum; 5O7J; -.
DR AlphaFoldDB; G3XD98; -.
DR BMRB; G3XD98; -.
DR SMR; G3XD98; -.
DR STRING; 208964.PA0928; -.
DR PaxDb; 208964-PA0928; -.
DR GeneID; 880882; -.
DR KEGG; pae:PA0928; -.
DR PATRIC; fig|208964.12.peg.963; -.
DR PseudoCAP; PA0928; -.
DR HOGENOM; CLU_000445_104_15_6; -.
DR InParanoid; G3XD98; -.
DR OrthoDB; 9797243at2; -.
DR PhylomeDB; G3XD98; -.
DR BRENDA; 2.7.13.3; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:PseudoCAP.
DR GO; GO:1900378; P:positive regulation of secondary metabolite biosynthetic process; IMP:PseudoCAP.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR019247; Histidine_kinase_BarA_N.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF09984; sCache_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5O7J, ECO:0007829|PDB:7N0E};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0007829|PDB:7QZ2, ECO:0007829|PDB:7Z8N};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002438};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..243
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 290..511
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 666..785
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 820..912
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 224..255
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 671
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:7QZ2"
FT BINDING 672
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:7QZ2"
FT BINDING 715
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:7QZ2"
FT BINDING 717
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:7QZ2"
FT MOD_RES 715
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 859
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 925 AA; 101054 MW; E6FC7B8C47A6AB8E CRC64;
MFKDLGIKGR VLLLTLLPTS LLAMVLGGYF TWVQLSDMRA QLIERGQLIA EQLAPLAATA
LARKDTAVLN RIANEALDQP DVRAVTFLDA RQERLAHAGP SMLTVAPAGD ASHLSMSTEL
DTTHFLLPVL GRHHSLSGAT EPDDERVLGW VELELSHHGT LLRGYRSLFT SLLLIAAGLG
VTALLALRMS RAINAPLELI SQGVAQLKEG RMETRLPPMG SNELDELASG INRMAETLQS
AQEEMQHNID QATEDVRQNL ETIEIQNIEL DLARKEALEA SRIKSEFLAN MSHEIRTPLN
GILGFTNLLQ KSELSPRQQD YLTTIQKSAE SLLGIINEIL DFSKIEAGKL VLENLPFNLR
DLIQDALTML APAAHEKQLE LVSLVYRDTP IQLQGDPQRL KQILTNLVGN AIKFTQGGTV
AVRAMLEDES DDRAQLRISV QDTGIGLSEE DQQALFKAFS QADNSLSRQA GGTGLGLVIS
KRLIEQMGGE IGVDSTPGEG AEFWISLSLP KSRDDNEEPG ASWAAGQRVA LLEPQELTRR
SLHHQLTDFG LEVSEFADLD SLQESLRNPP PGQLPISLAV LGVSAAIHPP EELSQSFWEF
ERLGCKTLVL CPTTEQAQYH ATLPDEQVEA KPACTRKLQR KLQELLQVRP TRSDKPHAMV
SGRPPRLLCV DDNPANLLLV QTLLSDLGAQ VTAVDSGYAA LEVVQRERFD LVFMDVQMPG
MDGRQATEAI RRWEAEREVS PVPVIALTAH ALSNEKRALL QAGMDDYLTK PIDEQQLAQV
VLKWTGLSLG QSLASMSRAP QLGQLSVLDP EEGLRLAAGK ADLAADMLAM LLASLAADRQ
AIRQARDNDD RTALLERVHR LHGATRYCGV PQLRAACQTS ETLLKQNDPA AAAALDELDK
AIEALADTAS ATTHLSSTSL DSSEL
//
