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Database: UniProt
Entry: A0A0N0J739_9PROT
LinkDB: A0A0N0J739_9PROT
Original site: A0A0N0J739_9PROT 
ID   A0A0N0J739_9PROT        Unreviewed;      1057 AA.
AC   A0A0N0J739;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=IP80_19240 {ECO:0000313|EMBL:KPF43695.1};
OS   beta proteobacterium AAP65.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF43695.1, ECO:0000313|Proteomes:UP000037849};
RN   [1] {ECO:0000313|EMBL:KPF43695.1, ECO:0000313|Proteomes:UP000037849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP65 {ECO:0000313|EMBL:KPF43695.1,
RC   ECO:0000313|Proteomes:UP000037849};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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:KPF43695.1}.
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DR   EMBL; LJHW01000045; KPF43695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0J739; -.
DR   STRING; 1523424.IP80_19240; -.
DR   PATRIC; fig|1523424.3.peg.3262; -.
DR   Proteomes; UP000037849; 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; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.450.350; CHASE domain; 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; IPR006189; CHASE_dom.
DR   InterPro; IPR042240; CHASE_sf.
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; IPR007895; MASE1.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF03924; CHASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF05231; MASE1; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM01079; CHASE; 1.
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; PS50839; CHASE; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000037849};
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..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        41..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          326..410
FT                   /note="CHASE"
FT                   /evidence="ECO:0000259|PROSITE:PS50839"
FT   DOMAIN          546..616
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          620..672
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          689..911
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          932..1049
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         982
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1057 AA;  111163 MW;  17BEF835D0B24872 CRC64;
     MEATAGPAVV LGTFIAYALA GGLALMLAGP PSYASPLYPS AGIALAAVLV HGRVALLGVM
     LGALAVNGGL ASMRGAPGLA SLALPLVISL GATLQAAVAA ALVRRRVSHP LVLDAPRDIL
     RFSLLGALLG CCVSASVATS ALVLLGELPL AAAASTWGTW WVGDAFGVLI GAPLALTLIG
     TPREDWRPRA RTLAVPTLAA VALLAAAMLE LSQLDRQRAQ AAFERDADRL VAAAEARLAV
     PLYALQALHS AASVQGRLDD RTLASASAWW TQQQPSPLRA LGYSERVPLA KLAAYEAEAR
     HEGKGSFRVF DRDNGQARTA DGEVLVLRHI APLEGNRTAL GVNVLSIPAA RLALQATLAS
     AEPAATGGFR LTQAEGDETG VVLYQALYRG PAGTEAERRA SFSGVVFVTV ATERAMAGLA
     AAARTPLRWC LVDTASGVAR PRLAGDMGCE TTAAPGEMLS TRRSLALGGR ALELRIEPGP
     GAAGGEKAAS WLLSLAGLAA VSLLGALLLT VTGHTRRTER AVQAGTSELR REIRERAAAE
     TALRESEERL RSILDHVPLG VVFLDPQGLV IEGNARFAAM AGQPAVAMRG VPVAAHVHAD
     DIPRVVALRR ALLEGQGAQV VEPVRLLQAD GPPLQVRVIA NALRSADGRL LRMVGVIEDI
     TEHLRLLESE NALQRAEAAN RAKSEFLSRM SHELRTPLNA MIGFAQLLGL DREHGLAPHQ
     REWTQQIQRA GWHLLEMINE TLDLARIESG AVQLKLAPLA LEPLVAACSA MVAAPAAQRG
     IQIGHVLDRD ARAVLADPMR LRQVLTNLLS NAVKYNAQGG TVSITAQRLA LPGGEMVELS
     VADTGLGMTG EQLGALFQPY NRLGREGSGI EGTGIGLVIS RRLAELMGGT LSARSEAGRG
     SVFTLRLPAA DADESPAPVY SDTSPAPYQQ RLVHYVEDNE TNIEVMRGVL AQRAQIQLKT
     SQLGLDGLAA IRAQQPDLIL LDMQLPDISG QELLRHLKQD DSVAHIPVVV VSADATTPAA
     AQALTAGAAH YVTKPLDVAQ FLQIVDTLLE SAETRWG
//
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