ID A0A0D8D533_9GAMM Unreviewed; 889 AA.
AC A0A0D8D533;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SG35_02905 {ECO:0000313|EMBL:KJE43579.1};
OS Thalassomonas actiniarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassomonas.
OX NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE43579.1};
RN [1] {ECO:0000313|EMBL:KJE43579.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5K-106 {ECO:0000313|EMBL:KJE43579.1};
RA Olonade I., van Zyl L.J., Tuffin M.I.;
RT "Genome sequence of Japanese sea anemone isolate Thalassomonas
RT actiniarum.";
RL Submitted (JAN-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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:KJE43579.1}.
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DR EMBL; JYNI01000003; KJE43579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D8D533; -.
DR STRING; 485447.SG35_02905; -.
DR PATRIC; fig|485447.4.peg.2924; -.
DR GO; GO:0016020; C: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; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 30..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 228..449
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 603..719
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 792..889
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 749..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 652
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 831
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 889 AA; 98409 MW; F780DF7EFBCF5001 CRC64;
MAYINYDHGL NQMLAKLSQN PKIKRARKRL IYYAWTGFFA NLIGGILIYL STFFGLVAQS
IHLINALTLY AIFFYTWVIL TIATRETITR RFSQKILMVQ IANSGVLLFF VLVFYPEIKT
TILVLWIMAF AFTFSFGTLK QSVMLSVLIF VFYVISLAVS GFFYKNAQEV ISELIFLCAF
IPTCAFISYV GAKLKKQRDN TQKAKLQLEE ALKVAAAASE SKSAFLANMS HEIRTPMNAI
INLSYLCLQS DLGARQRNYV EKVNKSAKSL LQIINDILDF SKVEAGKLHI EQADFSLDEM
LAHLAVIEVP KNKRKKLQLI FDVQPGTPIL LSGDLVRINQ VLFNLLSNAI KFTKSGRIVL
SIRVLQWQEK QVVIKFMVRD SGIGMAQEVA DKMFEPFSQA DTSTTRVFGG TGLGLVICKQ
LTELMGGRFE LLSEQGRGTR ASAILPVGLA SRPVLQQSTP ATNKQVLVSA QDDIALSAIE
HTLAAFAVCV TGRSSLDFDL DMMAEVDVIM IDESCPQTEI AAFFNRWVQL HQKSIMVIFV
SDQEGLPPEL AKYPLRHLQK PVYFTNFCDV LSGADKARGG QGHEHHQQFI LSANLYQQVG
KQRILLAEDN ELNQEIISDL LADSGCELHM VENGQQVLDL LEHQEIDVIL MDIQMPVMDG
IEATRLIRAA PKWRHIPIIA LTASAIKNDM EQGLAIGMNE YLTKPVIPKK LFAALTRCCP
PKTEIHDVEH DDFFPKDAGD RQSKISLEQQ DAAETGGMPG SNGEQALAEN SSRTVDFPGL
NVKAALRTCN GKEALFKKLI AGFADKFSAI DDDIKQALAQ GDCEQAKHLA HNLSGISANI
GALALAKVAA GIEKDLALTG GVSGPLPESL KGELQQVLHS IKRYLDNGV
//
