GACS_PSESY
ID GACS_PSESY Reviewed; 907 AA.
AC P48027;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Sensor protein GacS;
DE EC=2.7.13.3;
GN Name=gacS; Synonyms=lemA;
OS Pseudomonas syringae pv. syringae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1314807; DOI=10.1128/jb.174.9.3011-3020.1992;
RA Hrabak E.M., Willis D.K.;
RT "The lemA gene required for pathogenicity of Pseudomonas syringae pv.
RT syringae on bean is a member of a family of two-component regulators.";
RL J. Bacteriol. 174:3011-3020(1992).
CC -!- FUNCTION: Forms part of a two-component regulatory system
CC GacA/GacS(LemA). May be involved in lesion formation, swarming and in
CC the production of extracellular protease, syringomycin and N-acyl-L-
CC homoserine lactone (acyl-HSL). Required for pathogenicity on bean.
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:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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}.
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DR EMBL; M80477; AAA25877.1; -; Genomic_DNA.
DR AlphaFoldDB; P48027; -.
DR SMR; P48027; -.
DR PRIDE; P48027; -.
DR BRENDA; 2.7.13.3; 5193.
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..907
FT /note="Sensor protein GacS"
FT /id="PRO_0000074767"
FT TRANSMEM 9..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 182..234
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 281..502
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 658..777
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 814..907
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MOD_RES 284
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 707
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 853
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 907 AA; 99196 MW; 5B9F4663DAF3492C CRC64;
MLLLTILPAS LMAAMLGGYF TWMQLSELQS QLLQRGEMIA QDLAPLAANA LGRKDKVLLS
RIATQTLEQT DVRAVSFLDT DRTVLAHAGP TMISPSPIGS GSQLLSSTGT DATRYLLPVF
GSQRHLTSPI IPAEADTLLG WVELEISHNG TLLRGYRSLF ASLLLILTGL AFTATLAVRM
SRTINGPMSQ IKQAVSQLKD GNLETRLPPL GSRELDELAS GINRMAATLQ NAQEELQLSI
DQATEDVRQN LETIEIQNIE LDLARKEALE ASRIKSEFLA NMSHEIRTPL NGILGFTHLL
QKSELTPRQF DYLGTIEKSA DNLLSIINEI LDFSKIEAGK LVLDNIPFNL RDLLQDTLTI
LAPAAHAKQL ELVSLVYRDT PLALSGDPLR LRQILTNLVS NAIKFTREGT IVARAMLEDE
TEEHAQLRIS VQDTGIGLSS QDVRALFQAF SQADNSLSRQ PGGTGLGLVI SKRLIEQMGG
EIGVDSTPGE GSEFWISLKL PKAREDKEES LNIPLGGLRA AVLEHHDLAR QALEHQLEDC
GLQTIVFNNL ENLLNGVTAA HETPAAIDLA VLGVTALEIS PERLRQHIWD LENLNCKVMV
LCPTTEHALF QLAVHDVYTQ LQAKPACTRK LQKALSELIA PRAVRADIGP PLSSRAPRVL
CVDDNPANLL LVQTLLEDMG AEVVAVEGGY AAVNAVQQEA FDLVLMDVQM PGMDGRQATE
AIRAWEAERN QSSLPIVALT AHAMANEKRS LLQSGMDDYL TKPISERQLA QVVLKWTGLA
LRNPAPERQN EALEVHVGPL VLDHEEGLRL AAGKADLAAD MLAMLLASLD ADREAIRVAR
ANQDVHALIE RIHRLHGATR YCGVPQLRSA CQRAETLLKQ NAPHTEEALN DLDKAIIRLE
AEARVMA
