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Database: UniProt
Entry: A0A1I3MH02_9PSED
LinkDB: A0A1I3MH02_9PSED
Original site: A0A1I3MH02_9PSED 
ID   A0A1I3MH02_9PSED        Unreviewed;       984 AA.
AC   A0A1I3MH02;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216206_3278 {ECO:0000313|EMBL:SFI96050.1};
OS   Pseudomonas guineae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=425504 {ECO:0000313|EMBL:SFI96050.1, ECO:0000313|Proteomes:UP000243606};
RN   [1] {ECO:0000313|Proteomes:UP000243606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24016 {ECO:0000313|Proteomes:UP000243606};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOQL01000004; SFI96050.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3MH02; -.
DR   STRING; 425504.SAMN05216206_3278; -.
DR   OrthoDB; 9815750at2; -.
DR   Proteomes; UP000243606; 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; 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.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:SFI96050.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243606};
KW   Transferase {ECO:0000313|EMBL:SFI96050.1};
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..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        241..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        279..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        322..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        376..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        398..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        429..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        471..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          763..977
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   984 AA;  108333 MW;  BE88A14B34683788 CRC64;
     MLTSFSLSQL ILISAAYLLI LFGVAWISEH GLIPRWIIRH PLTYTLSLGV YASAWAFYGT
     VGLAYQYGYG FLASYLGVSG AFLLAPVLLY PILKITRTYQ LSSLADLFAF RFRSTWAGAL
     TTVFMLIGVL PLLALQIQAV ADSIGILTRE PVQERVALAY CGLIILFTIL FGARHIATRE
     KHEGLVFAIA FESVVKLVAI SIIGLYALYG VFDGPQDLQS WLVQNQASLS NLHTPLQEGP
     WRTLLLVFFA SAIVMPHMYH MTFTENLNPR AMVSASWGLP LFLLLMSLAV PLILWAGLKL
     GATTNPEYFT LGVGIAVNSQ TLALIAYVGG LSASSGLIIV TTLALSGMVL NHVVLPLYQP
     PAEGNIYRWL KWTRRALILL VIMAGYGFYL LLGAEQDLAN LGIVAFVATL QFLPGVLSVL
     YWPTANRKGF IAGLLAGVGV WVVSMLLPML GNLQGLYLPW FNVIYVLDDS SWHMAAIASL
     AANVLVFTLV SLFTEASQEE KSAAEACAVD NVRRPQRREL LANSPQEFAA QLAKPLGAKT
     AQHEVEQALR DLHLPFDEAR PYALRRLRDR IEANLSGLMG PSVAQDIVET FLPYKAGSET
     YVSEDIHFIE NRLEDYHSRL TGLAAELDTL RRYHRQTLQE LPMGVCSLAK DQEILMWNKA
     MEELTEIPAQ RVVGSRLSAL GEPWRGLLQN FIELPDEHLH KQSLALDGQT RWLNLHKAAI
     DEPLAPGNSG LVLLVEDLTE TQMLEDKLVH SERLASIGRL AAGVAHEIGN PITGIACLAQ
     NLREEREGDS ELTEISAQII EQTKRVSRIV QSLMSFAHSG SHQNSEEPVC LAQVAQDAIA
     LLALNRQSVD VQFFNLCDSD HWVIGDPQRL AQVLINLLSN ARDASPPSSA IRIKSEAFEH
     TVDLIVEDEG TGIPKAIIDR LFEPFFTTKE VGKGTGLGLA LVYSIVEEHY GQITIDSPAD
     PELQRGTRIR VSLPRHVEAT SLAT
//
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