ID Q8F9S9_LEPIN Unreviewed; 714 AA.
AC Q8F9S9;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 2.
DT 24-JAN-2024, entry version 128.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=LA_0111 {ECO:0000313|EMBL:AAN47310.2};
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN47310.2, ECO:0000313|Proteomes:UP000001408};
RN [1] {ECO:0000313|EMBL:AAN47310.2, ECO:0000313|Proteomes:UP000001408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601 {ECO:0000313|EMBL:AAN47310.2,
RC ECO:0000313|Proteomes:UP000001408};
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X.,
RA Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., Gu W.Y.,
RA Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., Wan M.,
RA Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., Qiang B.Q.,
RA Xia Q.C., Guo X.K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.M.,
RA Shi M.H., Chen Z., Xu J.G., Zhao G.P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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}.
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DR EMBL; AE010300; AAN47310.2; -; Genomic_DNA.
DR RefSeq; NP_710292.2; NC_004342.2.
DR RefSeq; WP_000058536.1; NC_004342.2.
DR AlphaFoldDB; Q8F9S9; -.
DR STRING; 189518.LA_0111; -.
DR PaxDb; 189518-LA_0111; -.
DR EnsemblBacteria; AAN47310; AAN47310; LA_0111.
DR GeneID; 61143455; -.
DR KEGG; lil:LA_0111; -.
DR PATRIC; fig|189518.3.peg.114; -.
DR HOGENOM; CLU_381207_0_0_12; -.
DR InParanoid; Q8F9S9; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR007895; MASE1.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF05231; MASE1; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AAN47310.2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001408};
KW Transferase {ECO:0000313|EMBL:AAN47310.2};
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 34..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 515..713
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 310..347
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 714 AA; 81337 MW; 2F6A84E84F916D05 CRC64;
MSLRFKEIVK ICGIIFISGM IYYVLALIGR KTAIYPSYAA AIWPASGAAL GFTLLFGNYA
VLGVFLASVL FNFGTGILSG DNLYLNFLIG FFSAFQSYVG KTVLTRKIPG YKISDRTQFV
FLFIFLEAIV CVINATGSVA SMYFLGEIDL SSIRQSWLTW WVGEVLGVYV GAPFILFWFR
GPYKLFRWKE FFESAILLFL IVFFSLTSFD LTTSVFFFNY SLGYVLVPLI LWSAFRLGER
ASSLAVILSS IIAIFGSIPT RFNAESIGES SILLQFFIAV LSITSLLVVS MVNERKEVED
QLRISHQSLE EKVEERTHEL LRSNEILREE IQEKNEARAA LEKSQTRYMG LFEHLPVAII
EADYSELKRV LDCLPSDIQG DIFSDYIETR PDFVRHCFNS IQVVGVNQET VNLLRVGSID
EVYKGWRFFF SQDNFKVFKR VLRKIREKSY FYEVEVGFRV KDNTRLDIKI RWSVPPGFES
SLSSVIVTLL DFTEIKSAER KLQLSLNEKE VMLKEIHHRV KNNLQVISSL LSMQSDYVQD
KQSLSVFIES QNRLRTMSMI HEELYQSENL GKIQYSVYIE KLLNQLFQVY GKSDSVVLVT
LLEPLDITVN RAIPIGLIIN ELVSNSLKYA FPEGRSIPNK PELRVSFSKS GENLEMRVED
NGIGMPFGFD LKDSNSLGLK LVNILVRQLG GKIDFSSDSK KGTQFKIHIP LSIG
//
