ID A0A1G3KXP9_9SPIR Unreviewed; 938 AA.
AC A0A1G3KXP9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-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=A2Y41_10370 {ECO:0000313|EMBL:OHD10370.1};
OS Spirochaetes bacterium GWB1_36_13.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802174 {ECO:0000313|EMBL:OHD10370.1, ECO:0000313|Proteomes:UP000177420};
RN [1] {ECO:0000313|EMBL:OHD10370.1, ECO:0000313|Proteomes:UP000177420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHD10370.1}.
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DR EMBL; MIAO01000098; OHD10370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3KXP9; -.
DR STRING; 1802174.A2Y41_10370; -.
DR Proteomes; UP000177420; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 193..235
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 265..317
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 317..389
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 444..514
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 518..570
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 636..938
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 561..592
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 938 AA; 106957 MW; 3DA68E223A637CA4 CRC64;
MENFFKTILN LIQNLTILFS LVFIYTFINP KLKKINRISQ KIILGIVFGL IAIVSMQVKI
SEVSGIIGRF EIPCVAGIFF GPLPAIITAV LSGISRYIIG GVGMLPGLGV IVTSALTGIL
IHKIWKKKVF HFKIIIFSGI GLILVVQGLL WALLIPHFWD IVHQILFSFI FFYPIDLALL
CFLIVYQSKR EFLEKRFETI FNKINDAVFI HEESSGIVVD VNETMLKMYG YSSKDEIIGK
KIDVFSADEK EYTQEEALQK ISLEQTAPFY WHAKKKNGDL FWVEVSLKKI VLSEEVYVIA
VVRDISQRKE TEEVLKTEKE LNEILIQSSP SFFVAIGSDG RVIKINQSML NSLGYSESEV
IGKDYLSLFV PNQDQIILKE IFKQIIDERK NTINVSRVLA KDGHVLVCEW HGIPVFHGQK
YDFFLGVGID ITEREKAVED FIKKEAQIKT LIDTIPDLVW LKDENGVYLE CNHRFEDFFG
AKKEDIIGKT DYDFVDKALA DFFRNKDRIA MEMGKPSINE EEIVFASDGH KEILETIKTP
VYGKNGQLMG VLGIGRNISE RKEKEVQIKE LNETLEQKVI ERTAQLEAAN EELDTSNQIL
IKNNIELEKA YDSLKTAQEK IIESAKMAAL GNLIAGIAHE MNTPLGAIVS SGNMVLDSLE
KATDLVYFDS LHLSEKEKKY FEILRKKALS FDFSEENTKD FRKRKKMLTR LLESKNIMEK
ELAEFLCEIG YSGEEEILDS LFDSKNYQKI IEMAYNLSHI SMSSKIIQMA SEKASKVVFA
LKTYSHHQNN EPLQKTDLKN SIETVLTLYH SQYKYRVEVV RNYEENLKVL SYPEKLNQVW
INLLNNALQA MKYQGKIEIG IQTKNGQALV SFEDNGPGIS KEIKNKIFEP FFTTKKAGEG
TGLGLDICRK IVEEIGGKID FESVPGKTVF YIYLKSED
//
