GTRS_PSEAE
ID GTRS_PSEAE Reviewed; 473 AA.
AC Q9HZ47;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sensor histidine kinase GtrS {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000269|PubMed:24920832};
DE AltName: Full=Glucose transport sensor {ECO:0000303|PubMed:22262100};
GN Name=gtrS {ECO:0000303|PubMed:22262100};
GN OrderedLocusNames=PA3191 {ECO:0000312|EMBL:AAG06579.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., 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.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., 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]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=22262100; DOI=10.1099/mic.0.056127-0;
RA O'Callaghan J., Reen F.J., Adams C., Casey P.G., Gahan C.G.M., O'Gara F.;
RT "A novel host-responsive sensor mediates virulence and type III secretion
RT during Pseudomonas aeruginosa-host cell interactions.";
RL Microbiology 158:1057-1070(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24920832; DOI=10.1093/nar/gku496;
RA Daddaoua A., Molina-Santiago C., de la Torre J., Krell T., Ramos J.L.;
RT "GtrS and GltR form a two-component system: the central role of 2-
RT ketogluconate in the expression of exotoxin A and glucose catabolic enzymes
RT in Pseudomonas aeruginosa.";
RL Nucleic Acids Res. 42:7654-7663(2014).
CC -!- FUNCTION: Member of the two-component regulatory system GtrS/GltR
CC involved in the regulation of glucose metabolism and transport, as well
CC as regulation of the exotoxin A gene expression (PubMed:24920832). GtrS
CC recognizes and binds 2-ketogluconate and 6-phosphogluconate via its
CC sensor domain, which accelerates GtrS autophosphorylation and
CC concomitant transphosphorylation and regulation of the response
CC regulator GltR (PubMed:24920832). {ECO:0000269|PubMed:24920832}.
CC -!- FUNCTION: Plays a key role during bacteria-host interactions and is
CC required for optimal colonization and dissemination in a mouse model of
CC infection (PubMed:22262100). Contributes to modulation of the type III
CC secretion system (T3SS) in response to host cells via the regulation of
CC the OprB transport system (PubMed:22262100).
CC {ECO:0000269|PubMed:22262100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:24920832};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:24920832}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced during infection of airway epithelial cells.
CC {ECO:0000269|PubMed:22262100}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:24920832}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene results in elevated
CC ingestion and reduced cytotoxicity of eukaryotic cells during
CC P.aeruginosa infection. {ECO:0000269|PubMed:22262100}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG06579.1; -; Genomic_DNA.
DR PIR; D83246; D83246.
DR RefSeq; NP_251881.1; NC_002516.2.
DR RefSeq; WP_003114839.1; NZ_QZGE01000019.1.
DR AlphaFoldDB; Q9HZ47; -.
DR SMR; Q9HZ47; -.
DR STRING; 287.DR97_4745; -.
DR PaxDb; Q9HZ47; -.
DR EnsemblBacteria; AAG06579; AAG06579; PA3191.
DR GeneID; 882906; -.
DR KEGG; pae:PA3191; -.
DR PATRIC; fig|208964.12.peg.3337; -.
DR PseudoCAP; PA3191; -.
DR HOGENOM; CLU_000445_89_27_6; -.
DR InParanoid; Q9HZ47; -.
DR OMA; EWLYIAS; -.
DR PhylomeDB; Q9HZ47; -.
DR BioCyc; PAER208964:G1FZ6-3251-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR CDD; cd00082; HisKA; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..473
FT /note="Sensor histidine kinase GtrS"
FT /id="PRO_0000454756"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24920832"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..197
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:24920832"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24920832"
FT DOMAIN 217..269
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 277..471
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 280
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 473 AA; 53049 MW; E88C53D1897B0864 CRC64;
MPRSLLGRML LLTLLAVLVA QGLSSLFWLS HLRSSQREGL LTSSRSLAYS MAASVSYFRS
LPLGYRPLVL DQLRSMGGTR FFVSLNDRPL EMRALPDTPN KQAVLEIVQD VLHQRLGKEV
ELQVEFVSPD ELRLFNGALK LDELPRSWAH YALTLEPVNP PVLVTQIRIG ESEWLYIASL
MPAPYVSLEP EGLQPQQVLS IVFTSLLLLL FTGLLMHWQS RPLKRLARAA RDLALGSPSA
ALEERGASEL VEVARAFNTM HERIDRYLNE RGQLFSAISH DLRTPITRLR LRVELLEDER
LQEKFGRDLD ELELLVKGAL QCVKDTDIHE NVESVDLNLL LQHIAEPYLA DGRVEVVGRA
AEPYPGKPLA LKRCIGNLLD NALKYGERAR LSLEDGPEAV VLHVDDDGPG VPEQRLEQIF
EPRFRLSPRG QGYGLGLGIA RNIAHTHGGE VSLQNRREGG LRVSLRLPRL GLE
