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Database: UniProt
Entry: A0A2K9LNY6_9GAMM
LinkDB: A0A2K9LNY6_9GAMM
Original site: A0A2K9LNY6_9GAMM 
ID   A0A2K9LNY6_9GAMM        Unreviewed;       995 AA.
AC   A0A2K9LNY6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Kalk_16120 {ECO:0000313|EMBL:AUM13861.1};
OS   Ketobacter alkanivorans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Ketobacteraceae; Ketobacter.
OX   NCBI_TaxID=1917421 {ECO:0000313|EMBL:AUM13861.1, ECO:0000313|Proteomes:UP000235116};
RN   [1] {ECO:0000313|Proteomes:UP000235116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GI5 {ECO:0000313|Proteomes:UP000235116};
RA   Kim S.-J., Rhee S.-K.;
RT   "Direct submision.";
RL   Submitted (AUG-2017) 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; CP022684; AUM13861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K9LNY6; -.
DR   KEGG; kak:Kalk_16120; -.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000235116; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000235116};
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        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        71..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..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..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        364..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        399..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        427..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          629..673
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          762..974
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   995 AA;  109604 MW;  2525703FAF2FB5D3 CRC64;
     MDFSVAQLFG IGVGYLLLFF LVAYLTEQGY IPARIVRHPA TYVLSLGVFA SAWAIYGAVG
     FAHDFGYNFL AYYLGISGAF MLAPIILAPI LKLTQTYQLG SLADLLSFRY RSPVVGAVVT
     ITMLVGIMPL LALQIQAVAD AIHILNEDTS PEMLAFAFVV LIIMFAILFG ARHISTREKH
     EGLVVAIAFE SLVKLVGFLL VGGIILFDVF GGPSGLNNWL EDHPEQLVSL YQPLEEGPWR
     ALVAAFFVAS VAMPHMFHMA FTENLNPRAI LTASWGLPLY LFLIALPVLI IVWAAAKLNI
     FSNPEYFTLL VPQAMESKWL AILGFAAGLS AASGVIIVCT LSLSAMFLNH LVLPMAPFYR
     RTNLYSWLLW MRRLLITAIV LVSYLFYVVM QNKHTLSELG FLAFVATMQF VPGLFGVLLW
     PKANKDGFLA GLAAGISVWL FGLLLPVLLG IQIHISAPLL INDLFPTPNN SYMVATFAIF
     INSTIFGIVS MLTESSPAEK QAAETCNVDN LRRPQRWELS ISSAREFVGR LAKPLGASTA
     RREVELALND LAMSLDETRP YALRRLRDQL ESNLSGLLGP SVAHEIMNTS VPYVIHTNDT
     SGQDIHFIES RLEEYHDKLT GLAGELDSLR RFHRQTLQDL PVGVCSLGSD GEVLGWNSAL
     ETITRISPDQ ILGSQISHLP QPWNQVFSQF IDVDSRNQQI EVELDGVQRW ISLHKAAIGL
     GKSKQAHSGQ VVVVEDTTEI KMLEHHVAHN ERLASVGKLA AGVAHEIGNP ITGIACLAQN
     LRYDSEAPAI LESADQILDQ TKRITRIVQS LVSFSHSGTT EVAMEPVYVH ECVQEAIDLL
     SLNKEVTQVA FTNLADASHC VKGDQQRLTQ VFINLLSNAR DAMNIDGEVK ILSHEKDHTI
     VIEVEDNGSG IPPDVLKRIY EPFVTTKDPG KGTGLGMSLV YSIIEEHYGQ ITIQSPLDSE
     NGGTRVTITL PRYTLLSEGN TTVDHEEQHE PHPDR
//
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