ID M6FR86_9LEPT Unreviewed; 821 AA.
AC M6FR86;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LEP1GSC038_1995 {ECO:0000313|EMBL:EMM72654.1};
OS Leptospira weilii str. 2006001855.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=996804 {ECO:0000313|EMBL:EMM72654.1, ECO:0000313|Proteomes:UP000012101};
RN [1] {ECO:0000313|EMBL:EMM72654.1, ECO:0000313|Proteomes:UP000012101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2006001855 {ECO:0000313|EMBL:EMM72654.1,
RC ECO:0000313|Proteomes:UP000012101};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hospenthal D.R., Murray C.K., Pimentel G.,
RA Wasfy M., Vinetz J.M., Sutton G.G., 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:EMM72654.1}.
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DR EMBL; AFJM02000037; EMM72654.1; -; Genomic_DNA.
DR AlphaFoldDB; M6FR86; -.
DR Proteomes; UP000012101; 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; 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; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR004358; Sig_transdc_His_kin-like_C.
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; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {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}.
FT TRANSMEM 185..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 443..664
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 695..812
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 744
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 821 AA; 94073 MW; 5C44B6B8825FBF37 CRC64;
MIRSFLTIYF SLSFAVPVFG ESLSLAPGKI SQLQNNSSFL SFIHYFTDSK GENFREKIFA
KDASLSFRNI PAEMFSLGFT EDTAWFYIPL KNDTSSDYYG KFEIYNPYLE KVDIHYRYGY
KDQIYEVLAG ANRVYEENFP VLDFYLRPGE EIQIVCAIKS GTPLRIPFVL ESEKKYNFTE
QFRSIAVGLT LGFGIAMGLY NLSLYFSFRA RSYLYYFIMI LFSTVYLTSW DGLALPLFKP
AHGQYYLSLA LVFIYVSTLF LFLFSLEFLY PEKKDKEAKI VTAIYVLSNL LLIPLSIFYP
IQLNQFSYYL GLIINLIIVY FCIVRIREGF QPAKKFLLIH MVFPIAGILA NLSTTGAISI
NYFSLHLLKL AFVSQSVLFS IMLVQRIKEL EFKLKEGLQS EIHKNIILLK KEIQQRRETE
WELIQAKEIA EKASKVKSSF LANMSHEIRT PMNGVLGMVQ LLGTTKLNDE QKEYIQILSV
SAKSLLQIIN DILDFSKIEA GKISLDKEVF SIRSVLDEIH DLLYPLAKQK RIGLRLEGKF
EIQEYVYGDQ LRLRQILWNL TGNGIKFTNR GEVVLSVSQK NISIDKISIE FRVSDSGIGI
PLEKQKQVFD AFSQSDTSTA RKFGGSGLGL SITKQLVELQ GGTLNLESKE GYGSKFTFAI
TYGIPSESEI EKIFEAEKTK DLESAYSNAT SKSMRILVAE DNETNCLLIE RALKKLGYDP
VVVHNGREVI EKMQLNVFDM ILMDIHMPEV DGMEATKWIR SQKQNAEFPI IIALTADVIE
SNKEMYISKG MNDYLAKPLD LPLLKKTLDF WFEHVKISHR K
//
