ID A0A2K4G4X3_9PSED Unreviewed; 982 AA.
AC A0A2K4G4X3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C1886_16245 {ECO:0000313|EMBL:POA18559.1};
OS Pseudomonas sp. FW300-N1A1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2075555 {ECO:0000313|EMBL:POA18559.1, ECO:0000313|Proteomes:UP000236411};
RN [1] {ECO:0000313|EMBL:POA18559.1, ECO:0000313|Proteomes:UP000236411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW300-N1A1 {ECO:0000313|EMBL:POA18559.1,
RC ECO:0000313|Proteomes:UP000236411};
RA Spencer S.J., Aaring A.B., Hendricks A., Penterman J., Chakraborty R.,
RA Alm E.J.;
RT "Whole genome sequencing of deep branching strains shows evolution and
RT exchange across a contaminated watershed.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000256|ARBA:ARBA00006434}.
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:POA18559.1}.
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DR EMBL; PPSF01000037; POA18559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K4G4X3; -.
DR Proteomes; UP000236411; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd10322; SLC5sbd; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 1.
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; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
DR PROSITE; PS50112; PAS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 628..672
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 761..975
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 982 AA; 107969 MW; BE89C29E2C7116B1 CRC64;
MSFSLTQMIL ISAAYLAVLF GVAWVSERGM IPRAIIRHPL TYTLSLGVYA SAWAFYGTVG
LAYQYGYGFL SSYLGVSGAF LLAPVLLYPI LKITRTYQLS SLADLFAFRF RSTWAGALTT
IFMLIAVLPL LALQIQAVAD SIGILTREPV QHRVALSFCA LITLFTIFFG SRHIATREKH
EGLVFAIAFE SVIKLIAIGG VGLYALYGVF DGPQQLELWL LQNQTALAAL HTPLQEGPWR
TLLLVFFASA IVMPHMYHMT FTENLNPRSL VSASWGLPLF LLLMSLAVPL ILWAGLKLGA
TTNPEYFTLG IGIAANNKAL ALLAYVGGLS AASGLIIVTT LALSGMALNH LVLPLYQPPA
EGNIYRWLKW TRRALIVAII MAGYGFYLML GAEQDLANLG IVAFVATLQF LPGVLSVLYW
PTANRRGFIA GLMAGVLVWL VTMLLPLVGN LQGFYIPLLN MIYVLDDTSW HMAAIASLAA
NVLIFTLVSL FTNASTEEAS AAEACAVDNV RRPQRRELHA ASPQEFATQL AKPLGAKAAQ
KEVEQALRDL YLPFDERRPY ALRRLRDRIE ANLSGLMGPS VAQDMVETFL PYKAGGENYV
TEDIHFIESR LEDYHSRLTG LAAELDALRR YHRQTLQELP MGVCSLAKDQ EILMWNKAME
ELTGIAAQRV VGSRLSTLSE PWKELLQGFI NVPDEHLHKQ HLALDGQTRW LNLHKAAIDE
PLAPGNSGLV LLVEDLTETQ MLEDKLVHSE RLASIGRLAA GVAHEIGNPI TGIACLAQNL
REEREEDGEI TEISGQIIEQ TKRVSRIVQS LMSFAHAGSH QHNDEPVCLA EVAQDAIGLL
ALNRRNFEVQ FFNLCDPEHW VDGDPQRLAQ VLINLLSNAR DASPAGSAVR VKSEASEHTI
DLIVEDEGSG IPSSIMDRLF EPFFTTKDPG EGTGLGLALV YSIVEEHYGQ ITIDSPADTQ
SQRGTRIRVT LPRHVEATSA VN
//
