GACS_PSEPH
ID GACS_PSEPH Reviewed; 917 AA.
AC Q9F8D7;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Sensor histidine kinase GacS;
DE EC=2.7.13.3;
GN Name=gacS; Synonyms=lemA;
OS Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1124983;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RA Blumer C., Carruthers F., Mattart A., Reimmann C., Pechy M., Pessi G.,
RA Heeb S., Haas D.;
RT "Pseudomonas fluorescens CHA0 sensor kinase (gacS) gene.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=10570200; DOI=10.1073/pnas.96.24.14073;
RA Blumer C., Heeb S., Pessi G., Haas D.;
RT "Global GacA-steered control of cyanide and exoprotease production in
RT Pseudomonas fluorescens involves specific ribosome binding sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14073-14078(1999).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=11807065; DOI=10.1128/jb.184.4.1046-1056.2002;
RA Heeb S., Blumer C., Haas D.;
RT "Regulatory RNA as mediator in GacA/RsmA-dependent global control of
RT exoproduct formation in Pseudomonas fluorescens CHA0.";
RL J. Bacteriol. 184:1046-1056(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=14622422; DOI=10.1046/j.1365-2958.2003.03774.x;
RA Valverde C., Heeb S., Keel C., Haas D.;
RT "RsmY, a small regulatory RNA, is required in concert with RsmZ for GacA-
RT dependent expression of biocontrol traits in Pseudomonas fluorescens
RT CHA0.";
RL Mol. Microbiol. 50:1361-1379(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=15601712; DOI=10.1128/jb.187.1.276-285.2005;
RA Reimmann C., Valverde C., Kay E., Haas D.;
RT "Posttranscriptional repression of GacS/GacA-controlled genes by the RNA-
RT binding protein RsmE acting together with RsmA in the biocontrol strain
RT Pseudomonas fluorescens CHA0.";
RL J. Bacteriol. 187:276-285(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=16286659; DOI=10.1073/pnas.0505673102;
RA Kay E., Dubuis C., Haas D.;
RT "Three small RNAs jointly ensure secondary metabolism and biocontrol in
RT Pseudomonas fluorescens CHA0.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17136-17141(2005).
CC -!- FUNCTION: Member of the two-component regulatory system GacA/GacS which
CC controls the expression of secondary metabolites and extracellular
CC products. Activates GacA by phosphorylation (Probable). GacA acts
CC (probably primarily) by activating expression of CsrA1 and CsrA2
CC antagonist small RNAs (sRNA) RsmX, RsmY and RsmZ which bind to and
CC prevent translation repression by CsrA1 and CsrA2 (PubMed:11807065,
CC PubMed:14622422, PubMed:15601712, PubMed:16286659). Involved in the
CC regulation of secondary metabolism and in the synthesis of the
CC antifungal factors cyanide, 2,4-diacetylphloroglucinol and pyoluteorin
CC (PubMed:15601712). Exercises positive post-transcriptional control over
CC the hcnABC and aprA genes; acts upstream of CsrA2 (rsmA)
CC (PubMed:10570200). Controls expression of CsrA1 and CsrA2 antagonist
CC sRNAs RsmX, RsmY and probably RsmZ (PubMed:11807065, PubMed:14622422,
CC PubMed:15601712, PubMed:16286659). Probably controls expression of
CC csrA1 (rsmE) and csrA2 (PubMed:15601712). {ECO:0000269|PubMed:10570200,
CC ECO:0000269|PubMed:11807065, ECO:0000269|PubMed:14622422,
CC ECO:0000269|PubMed:15601712, ECO:0000269|PubMed:16286659, ECO:0000305}.
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 inner membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- PTM: Activation requires a sequential transfer of a phosphate group
CC from a His in the primary transmitter domain, to an Asp in the receiver
CC domain and to a His in the secondary transmitter domain. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Greatly decreased expression of aprA, hcnA and
CC phlA (PubMed:10570200, PubMed:11807065, PubMed:14622422,
CC PubMed:15601712). Partially suppressed by a deletion of csrA2 (rsmA)
CC (PubMed:10570200, PubMed:15601712). Fully suppressed by deletion of
CC csrA1 (rsmE) and csrA2 (PubMed:15601712). Its deletion is also
CC suppressed by overexpression of small RNAs (sRNA) RsmZ and RsmY
CC (PubMed:11807065, PubMed:14622422). Loss of expression of sRNA RsmY
CC (PubMed:14622422). Loss of protection of cucumber plants from fungal
CC infection (PubMed:14622422, PubMed:16286659).
CC {ECO:0000269|PubMed:10570200, ECO:0000269|PubMed:11807065,
CC ECO:0000269|PubMed:14622422, ECO:0000269|PubMed:15601712,
CC ECO:0000269|PubMed:16286659}.
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; AF246292; AAG13658.1; -; Genomic_DNA.
DR RefSeq; WP_011062714.1; NZ_LS999205.1.
DR AlphaFoldDB; Q9F8D7; -.
DR SMR; Q9F8D7; -.
DR STRING; 1124983.PFLCHA0_c45240; -.
DR GeneID; 57477528; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5002; Bacteria.
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 CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 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 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; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 2.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..917
FT /note="Sensor histidine kinase GacS"
FT /id="PRO_0000442646"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 192..244
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 291..512
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 668..787
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 824..917
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MOD_RES 294
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 717
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 863
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 917 AA; 100476 MW; 294EB086E006DF85 CRC64;
MLKKLGIKGR VLLLTLLPTS LMALVLGGYF TWMQLSDLQT QLLQRGEMIA EQLASLVAPA
MGNHNTQMLE RIATQALEQQ DVRAVSLLAP DRSLLAHAGP SMLNPPPAGN SSHMMQRSGS
DATRYQLPVF GRHRNLAGDL IPDESDRLLG WVELELSHSG MLLRGYRSLF ASLLLIAAGL
AGTALLAVRM GRTINNPLTQ IKQAVAQLKD GNLETRLPPL GSQELDELAS GINRMASTLQ
NAQEELQHSI DQATEDVRQN LETIEIQNIE LDLARKEALE ASRIKSEFLA NMSHEIRTPL
NGILGFTHLL QKSELTPRQL DYLGTIEKSA DSLLGIINEI LDFSKIEAGK LVLDSIPFNL
RDLLQDTLTI LAPAAHAKQL ELVSLVYRDT PLSLVGDPLR LKQILTNLVS NAIKFTREGT
IVARAMLEEE HEDSVQLRIS IQDTGIGLSN QDVRALFQAF SQADNSLSRQ PGGTGLGLVI
SKRLIEQMGG EIGVDSTPGE GSEFWISLNL PKTRDDAEDL PGPPLLGRRV AVLENHELAR
QALQHQLEDC GLEVTPFNTL EALTNGITGV HQSEQAIDLA VLGITTNDMS PERLSQHIWD
LEHLGCKVLV LCPTTEQTLF HLSVPNPHSQ LQAKPACTRK LRRALSDLVT PRRARSEPEE
TLSSRAPRVL CVDDNPANLL LIQTLLEDMG AKVLAVDNGY AALNAIQTEP FDLVMMDVQM
PGMDGRQSTE AIRQWESERH GTPLPIVALT AHAMANEKRA LLQSGMDDYL TKPISERQLA
QVVLKWTGLA LRNQGPERAS ERPELGLELQ VLDQDEGLRL AAGKADLAAD MLAMLLASLD
ADREAIKAAR AANDQNALIE RVHRLHGATR YCGVPQLRAA CQRSETLLKQ EDAKAFAALD
ELDHAIGRLA AEARTNA
