ID A0A0N0E5U4_9PSED Unreviewed; 1200 AA.
AC A0A0N0E5U4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PF66_00643 {ECO:0000313|EMBL:KPA92902.1};
OS Pseudomonas fuscovaginae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA92902.1, ECO:0000313|Proteomes:UP000037931};
RN [1] {ECO:0000313|EMBL:KPA92902.1, ECO:0000313|Proteomes:UP000037931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA92902.1,
RC ECO:0000313|Proteomes:UP000037931};
RX PubMed=26422147;
RA Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA Cruz C.V., Oliva R.;
RT "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL PLoS ONE 10:E0139256-E0139256(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPA92902.1}.
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DR EMBL; JSYZ01000002; KPA92902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0E5U4; -.
DR STRING; 50340.PF66_00643; -.
DR PATRIC; fig|50340.43.peg.2650; -.
DR Proteomes; UP000037931; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd13705; PBP2_BvgS_D1; 1.
DR CDD; cd13707; PBP2_BvgS_D2; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00062; PBPb; 2.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:KPA92902.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 575..647
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 719..942
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 963..1082
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1100..1200
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1012
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1139
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1200 AA; 132792 MW; 62657224BE60E905 CRC64;
MAFPGRSIYS ILAWLSWVML ASLPGELMAA QGLPFNLPAS FVELPRLPLG ADERRWLGND
RRLRVGISVA DYEPIDITSD RNRYQGISAD YVALIRDRLG VQVEVLGFVE RDQAVEALLE
GQIDVLTSAN GFERGFPELA FSSEYMPDRS VIVSRSETPN PDDLRGRKVL LLEGYADAAV
VHATYPQSRI ILAPTLYSAL EALLQGEVDA FIGNEVIVRA YKTLRPYMGL QIRGQSALPP
IGFAFATRKS EPLLGALIQR VLDSLDEAVR REILARWTTG FGSDIAQPRV ELTAAEQAWI
DSHPRVSVAS QQYPPYIYKD VHNRWVGLNA DLLARISRMT GLQFVFDESF STVQTLEMLK
DGRALMNGSL AESPERKAFL NFTYAFGGSS WVFVVPVDAP PLSSLSQLAG RVLALPEEHA
LQAMIRREYP DVVLRGVRTQ EEARALVESG AAAATIQSDT LAYLHPPGRL KVGRSVEGLW
SADSFSVAKS SPELLGILNK SLEAFPVAEL RALRIKWLGA VPVAAPPSVW KRVPRWAYGL
AVALLVVGGV SLIWNRRLNV QIRQRRQAER QLSDRLAFQR ALLDGIPDPI FVRDLQGRLI
SCNRSYEQRL ATTLEQVRGR RITEEGLLLP AVAQALHDDF LSLLENQQPV FSDRTLEFLN
CSIDVYLWMV PFHSAGAQLQ GLLGGWIDIT ERKQLEVQLT EARRQAERAS QAKSAFLATM
SHEIRTPMAA IIGLLEVERE QALARGQVFS QGLQVAYQSA RELTALIGDS LDLAKIEAGG
MRLVPQPTDL RNLLEGVVQL FEALARDKGV VLSLGIDPLL ASLYWLDPLR LRQILHNLIG
NALKFTSRGF VRVRVLRCAQ VAGTDRLRID IEDSGRGIGP EQQAMLFSPF VQAHGDADAG
HEGTGLGLSI CKQLVELMDG SIELESQPGL GTRVHIELAF RRETQPVLPA PSNGARCRLP
CLNVLIIDDL SANRLVLQQQ LGFLGQNVEA CQTAQAALQA WQGRHFDLVI SDCNMPGMSG
YQLARALRQL ETEAQRPPCM IVGCTANAMS DERQRCQQAG MNDLLVKPVL LDDLTRLLTQ
IVPRESSFDI QTLIDMTHAD AGVLQHMLLE LWRNLRDERA ELQSRLGLDD WDGVAACVHR
LKGIACLVDA IALAQACVDM DHCVRLRQPE QLPATGQVLK AVIDRMIADI EPNLQEKPAL
//
