ID   A0A1Q2GW13_9GAMM        Unreviewed;       660 AA.
AC   A0A1Q2GW13;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B0W48_05280 {ECO:0000313|EMBL:AQP99267.1};
OS   Pseudoalteromonas aliena.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=247523 {ECO:0000313|EMBL:AQP99267.1, ECO:0000313|Proteomes:UP000188243};
RN   [1] {ECO:0000313|EMBL:AQP99267.1, ECO:0000313|Proteomes:UP000188243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EH1 {ECO:0000313|EMBL:AQP99267.1,
RC   ECO:0000313|Proteomes:UP000188243};
RA   Kim E., Heo E., Kim H., Kim D.;
RT   "Complete genome sequence of the cold-active Pseudoalteromonas aliena
RT   strain EH1 isolated from Arctic seawater.";
RL   Submitted (FEB-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};
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DR   EMBL; CP019628; AQP99267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2GW13; -.
DR   STRING; 247523.B0W48_05280; -.
DR   KEGG; paln:B0W48_05280; -.
DR   Proteomes; UP000188243; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
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; 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; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AQP99267.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:AQP99267.1}.
FT   DOMAIN          130..244
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          270..340
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          428..648
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   MOD_RES         179
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   660 AA;  73836 MW;  B6B744390792E0BF CRC64;
     MIRKILIVDS SSVIAMRVKV LLELIGCEVE LIHFSMLKMY TNMSCYDLIV IAHGVPVTAI
     AYLVEKVPQE RFMLLAPKAE SGQQLTTFSE LNHVVPNATV VYPFFSNKEI TSLLESLLEI
     GSNHILQLPT ILLVDHIPER LENMKNSLVG AHIKTYTATN FEEALEVVTN RDLDILISDF
     SLGDTTGLEI FSKLKVEYPR CRCLLFTSRS DQVSMIEAIR QGVEDVLIKP LNDNILLQSV
     HKLWQTELLQ RHNTELVERL QDTVDALIEK DSLLQVIYKN TPDAIMLFER DGNVIEANNS
     CLKLFNLTFN KLENKSVFNF LDSDSSAIIK DKISTLNSNR QFSCDLYLSK TAGGYIPLVG
     SFNEIDHHGE IALAVIFKNV THLKQKEELL LEAKDILEEQ VRARTSQLEH AKNVAEAANL
     SKSEFLANMS HELRTPMHSI LSFARFGLDK LEAGDLAKEK LLKYLSRIES SGERLLSLLN
     NLLDLSKLDV GKFPFNPRSN NLANIIKMSI DDVAGTAMEK EIEIVFITQP PAVVAQCDEE
     QINQLLRNVL GNALKFSDRK SKITVNLESD NGFAIIEVVD DGVGIPEDEL EHIFTKFVQS
     SKTNSGAGGT GLGLALCREF VSLHQGDIRA INNENGGATI CIQFPLEIKQ DEHSENEELA
//