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Database: UniProt
Entry: H0J116_9GAMM
LinkDB: H0J116_9GAMM
Original site: H0J116_9GAMM 
ID   H0J116_9GAMM            Unreviewed;       996 AA.
AC   H0J116;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=MOY_06610 {ECO:0000313|EMBL:EHK61330.1};
OS   Halomonas sp. GFAJ-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK61330.1, ECO:0000313|Proteomes:UP000004512};
RN   [1] {ECO:0000313|EMBL:EHK61330.1, ECO:0000313|Proteomes:UP000004512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK61330.1,
RC   ECO:0000313|Proteomes:UP000004512};
RX   PubMed=22408239; DOI=10.1128/JB.06664-11;
RA   Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT   "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL   J. Bacteriol. 194:1835-1836(2012).
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:EHK61330.1}.
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DR   EMBL; AHBC01000025; EHK61330.1; -; Genomic_DNA.
DR   RefSeq; WP_009097899.1; NZ_CP016490.1.
DR   AlphaFoldDB; H0J116; -.
DR   STRING; 1118153.MOY_06610; -.
DR   KEGG; hag:BB497_01750; -.
DR   PATRIC; fig|1118153.6.peg.1333; -.
DR   eggNOG; COG5002; Bacteria.
DR   OrthoDB; 8573350at2; -.
DR   Proteomes; UP000004512; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd12914; PDC1_DGC_like; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR033479; dCache_1.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004512};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          308..361
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          366..442
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          455..507
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          511..730
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          750..866
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          875..989
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         799
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         923
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   996 AA;  109745 MW;  EAE6D3047C9D2C58 CRC64;
     MLKIPLSVRI VLLVFATSGI LVGGILVTVY QVMVADYESI VVEREASEIR RLASELELSQ
     QQRKLGLEAF ATRLLNDDGR LRSDQELQTL LEQPSVAGDL FPDGLLVFDA DGTAIAENRH
     VPGRIGTNYA DRPHFQRAWQ TKDAVISEPI IGRATGLPLI SYLQPMLSSD DRLMGYVGGV
     LDLSSTPLID NFSLEEAESS TTLIIDPRHR LYVSMLERVD TVASLPDDGA DAFVDAALAL
     NPPGTIVEYQ QQRYLTASQQ LDSLGWVVLR AIPYEKAIAP VKASFRQFLW IALFAMVLVA
     LVGAWVARSL THPIERITRR IEQMADHARF DDDFRERGGP EARALARAMN RLAYERKAAD
     TAVRNAERFL FNILEAASEV AIIATDTNGM ITAFNKGAEN MLGYSKADMV GKQTPAILHL
     KDEVELRSEQ LSAELDRTVE GFRVFVEHAE RDGSETREWT YVHKSGRRIP VSLVVTPMRD
     SADNISGYLG IAEDITARKQ ADKLKSEFIS TVSHELRTPL TSISGALGLM VGGAFGEMPE
     KAQKLLMTAH RNSKRLAHLI NDLLDIEKIA AGKLHFDMQV HALAPLIEQA LEANRHYGSE
     NGVTLLLADE SPDLMVNVDP SRLMQVLANL LSNAIKFSPE GGEVTLTVET SNHNAVVSVI
     DRGPGIADSF RSKVFQRFAQ ADSSDTRAKE GTGLGLAITR ELIEHMGGRI DFESTEGEGS
     RFFFELPLAQ TAVKASQPLE MDAENRDAPR ILVVEDDKDV ATLLSMMLSD AGYRVDIAFN
     GAEALSVLQN TQYDLVSLDL MLPDTSGLEI IRTLRGHPDT ADLPIVVVSA KVEQGRLAIN
     GDATNIDWLA KPIDQLRLID MVQQQLSANR EHHPRVLHVE DDLDLHEVVA AMAGESFTFE
     AAYTLESARS RLKEQAYDVV LLDIGLPDGS GWTLIPEIRA SQPEAKIVIL SGSDMTHQQH
     EQVEAVLLKS RLSADTLIDG IKARIRSTRL SRDKLS
//
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