ID A0A259FM64_9PROT Unreviewed; 710 AA.
AC A0A259FM64;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B7X87_04230 {ECO:0000313|EMBL:OZA39502.1};
OS Hydrogenophilales bacterium 17-64-34.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970527 {ECO:0000313|EMBL:OZA39502.1, ECO:0000313|Proteomes:UP000216129};
RN [1] {ECO:0000313|EMBL:OZA39502.1, ECO:0000313|Proteomes:UP000216129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17-64-34 {ECO:0000313|EMBL:OZA39502.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-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};
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:OZA39502.1}.
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DR EMBL; NCIL01000003; OZA39502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259FM64; -.
DR Proteomes; UP000216129; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
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; 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; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF00989; PAS; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OZA39502.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 299..351
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 363..411
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 493..704
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 339..370
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 710 AA; 76997 MW; 295AB3729060CE6D CRC64;
MRSLIVLAFV VGLLLLTLLF QASGDSAGFS DSLPILFLGG SVLGGVLLGL LGWRMWWLQK
RIRRGVFGAK LTLKLLLMFG VVALLPVLMV YGASVFFLNR SIETWFDVRV DNALASGVNL
GQAALDDLLQ DLDKKAQRIA LSLSDEGAGS MITALSTLRE QSAVQELTLF DERGGLVAHV
GGERGTLLPL LPDRTLLWQV RQQQPYSGIE EAGDRGLVMR VLVPVYTASF SGETRVLQLV
QPVPASLARD AQAVQEAYRE YQQISLSRLG LKRIYGAALT LTLLLALLLT FVIAYLLSDR
LGAPLRTLAR GTRAVAKGDF SQMPSVASRD ELGVLIQSFN RMTRQLSEAR EEVAQNHQET
EQAKAFLERV LANLSSGVVV LDEDQRIRTA NSAASQILGA PVGELEGRLL VALGVPQSPL
RAFGETVAKR FAEQAGEWSE QIDYTEHGDK QALLLRGTHL PAGVERGYVL VFDDMTKLID
AERNAAWSEV ARRLAHEIKN PLTPIQLSAE RIARKLGGKL APPDVEFLER ATQTIVNQVA
AMKSMVDAFA GYARMPRAKL APLDLNALVR EILALYDGKS LGLELHLDPA LPPVVGDSTL
LRQVIHNLLQ NAQDALADHA APRVEVSTSL SADAVCLAVN DNGGGFPEHL MARLFEPYAT
TKAKGTGLGL AIVKKIVEEH QGRIQIENLK TGGAAIRIAL PLHQANGGHT
//
