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Database: UniProt
Entry: A0A3F2V5A9_9GAMM
LinkDB: A0A3F2V5A9_9GAMM
Original site: A0A3F2V5A9_9GAMM 
ID   A0A3F2V5A9_9GAMM        Unreviewed;       596 AA.
AC   A0A3F2V5A9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=D6160_09075 {ECO:0000313|EMBL:RLP54950.1};
OS   Ketobacter sp.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Ketobacteraceae; Ketobacter.
OX   NCBI_TaxID=2083498 {ECO:0000313|EMBL:RLP54950.1, ECO:0000313|Proteomes:UP000280615};
RN   [1] {ECO:0000313|EMBL:RLP54950.1, ECO:0000313|Proteomes:UP000280615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BinD {ECO:0000313|EMBL:RLP54950.1};
RA   Xu J.;
RT   "Metagenomic reconstruction reveals the metabolic diversity of the novel
RT   genus Ketobacter and the trajectory of genomic evolution within the
RT   Alcanivoraceae family.";
RL   Submitted (SEP-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   -!- 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:RLP54950.1}.
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DR   EMBL; RAHY01000005; RLP54950.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F2V5A9; -.
DR   Proteomes; UP000280615; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd18773; PDC1_HK_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR033479; dCache_1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR   PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:RLP54950.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280615};
KW   Transferase {ECO:0000313|EMBL:RLP54950.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          339..391
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          396..469
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   COILED          372..399
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   596 AA;  66464 MW;  A12B5B68257C46B1 CRC64;
     MDRREPRRWF APTIQNKLLA VMLVVALTPL MVFGALAYFK SRETVINQVG ERLQAASLLA
     MSQIDRTFGF SLENIRSWAD LDTLQAVERG DPEGSISHML GDYQKAYGVY NTLVAVDEDA
     SVVAAGDPAL LGVSVTSADW YKRVMASGKP YMAPLRYDSD LGGYGVSLAV PIFKKYSDGY
     IIGVLKASLD WRELLQQVTA IEVVPEGQVP DGYAVLIDSE GYILAAPDFI LFSMESTLPE
     AGMARVYDSR WWVAENPMLL DRVLKRPGHR YIRRGNDELM LVNMPASEFR YIGKTGWSLV
     LVRNAKSALQ DIEYIRERAF LIGIITVLLI GLVAYIMSRQ IGSPITRLSR WAEQLSHGSL
     DSNISLRSND ELAQLASALD NMRRNLKKYL DELFDSKERY QSIISSIDCV VWEAHINPLK
     VTLLSGQVDH VLGRSPDQVL SHLDSWQSLV HSDHHSLLID ACTTAIERGT DTYVEFKFLH
     GNGNWMWVKA LISVTIEDLG VVGLRGVVVD INDIVIAAEE MAEARDIALK TAEDKSRFMA
     IVSHEIRTPI NGMLGMLDML SGQAGVDEQQ QTLSMAKRSG RNLLALVDEV MDFSRL
//
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