ID M6DKN3_9LEPT Unreviewed; 598 AA.
AC M6DKN3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LEP1GSC192_1664 {ECO:0000313|EMBL:EMK01879.1};
OS Leptospira sp. B5-022.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1242992 {ECO:0000313|EMBL:EMK01879.1, ECO:0000313|Proteomes:UP000011981};
RN [1] {ECO:0000313|EMBL:EMK01879.1, ECO:0000313|Proteomes:UP000011981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B5-022 {ECO:0000313|EMBL:EMK01879.1,
RC ECO:0000313|Proteomes:UP000011981};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Galloway R.L., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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 -!- 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:EMK01879.1}.
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DR EMBL; ANIJ01000006; EMK01879.1; -; Genomic_DNA.
DR AlphaFoldDB; M6DKN3; -.
DR STRING; 1242992.LEP1GSC192_1664; -.
DR PATRIC; fig|1242992.3.peg.606; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000011981; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 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 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; IPR004358; Sig_transdc_His_kin-like_C.
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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; 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 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 305..357
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 374..598
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 598 AA; 68647 MW; FB588672E430C1A2 CRC64;
MKWFPFRIEE ENRYYLRDLL ILSGVIFIAV LAAELIHFRN SESIDIVDRI LIYVYYTVPL
VVLFLILSYF YRNRRNLETG RLKSSIRYRL SLSFLFIAML PSFPVFLLTS NVIGRVFEGF
YGLDIAQALE AGDHFVRKEL EPEKNNLLEK AKLFRNLVKR ENPNPNLLTN RANELDLISN
PNYYVGWYDN NVPALENRSL KLTISPEEFT SFGTEGISEK LILSQSLSFY LLKIESLNPS
KFLILGKRVF HGEESKAYSF INTRKNYITA DLTKEKLPYE VRLTITLLTV FAFLLSIFFS
LVFARKISRP IIDLANATQK VSLGDTDINL PLTEGGEIGA LVESFNQMVK DLKSKNEELM
HSQRIAAWKE VAQRMAHEIK NPLTPIQLSA ERIRRKLNSE VPEEFQEIVT KGSETIVGQV
KILEHLVNEF SEFARMPAPR LINQHLEPVV LESAKLFEHT PGIQIELNFA KNLPEIFLDK
KLFLGIMNNL FKNAVEAIEK RRQRGDSSFF QGKVRISTVL EKRIMRRSVV LLVEDNGIGI
TPEYRSKVFE PYYSTKDEHV SGIGLAIVQK TVIDHNGHIS VDSSELGGCK FRIELPVA
//
