ID M6ZXD5_LEPIR Unreviewed; 900 AA.
AC M6ZXD5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LEP1GSC124_3611 {ECO:0000313|EMBL:EMP08967.1};
OS Leptospira interrogans serovar Pyrogenes str. 200701872.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193029 {ECO:0000313|EMBL:EMP08967.1, ECO:0000313|Proteomes:UP000012117};
RN [1] {ECO:0000313|EMBL:EMP08967.1, ECO:0000313|Proteomes:UP000012117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701872 {ECO:0000313|EMBL:EMP08967.1,
RC ECO:0000313|Proteomes:UP000012117};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA 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:EMP08967.1}.
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DR EMBL; AKWN02000084; EMP08967.1; -; Genomic_DNA.
DR AlphaFoldDB; M6ZXD5; -.
DR BioCyc; LINT1193029:G11R4-799-MONOMER; -.
DR Proteomes; UP000012117; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; cd00156; REC; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 250..470
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 513..626
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 635..751
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 781..898
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 157..236
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 562
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 684
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 831
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 900 AA; 102209 MW; DE9900BF205A4210 CRC64;
MTNGQNFLNE KLRGDKTESV LAKDVITFLS NYLNANVGAI YLCDDSECSL SVFGKYGFIS
ENRSSERFAL NEGLIGQVAA EQKRIFLTDV EEGSLRILSG ILDTKPKQIL IVPFVFEGKT
QGVIELGKLD SFSPSEIEFI ESSVQSIGIS FNSARARRKI QELLEQTRIQ SEELQTQQEE
LRQMNEELEE QTQVLRQQQE ELKVSNEELE EQTHILEMKN KEVELAKSDI EQKTKQLELS
GKYKSEFLAN MSHELRTPLN SLLILSKDLA DNKRKNLSED QVESANIIYK SGHDLLVLIN
DVLDLSKIES GKMSVNLERV VLRKFAKELM STFKLQATEK KLDLDLIFDD DLPEVIRTDS
HRLNQILKNL ISNALKFTER GKVQVEIKKQ NKDKILFSVI DSGIGIPEEK HSAIFEAFQQ
ADGSTSRKYG GTGLGLSISR ELAKLLGGEI FLKSKVNQGS TFSLSLPIET NEISISEKEN
EVFHNSVDSI QNEFINYPTL QDDRNQIGEN DKVLLVIEDD LKFASVLIKQ ANEKGFKCIS
AATGEDGLIL TRKYKPHAII LDLDLPGIKG QTVLNELKAD QSIRHIPVHI VSANEYSLEL
IRGGAVEHIR KPIHKKELDE AFNRIENFIN RKMKNLLIIE DDFNSRKMML KLIGNGDVKC
FEADSGKEAL RVYAENHFDC IVLDIGLPDM SGFELIQEME KIKNGRIPPI VIYTGKELTK
EEDKELQKYS ESIIIKGIKS EERLLDETAL FLHRMINDLP ESKQNIINNL YDKDSVLFQK
KILLVDDDMR NVFALSKILS EKGMNVLKAE DGNSALELLS KNEDVDLVLM DIMMPEMDGY
ETMKKIREIS KYKNLTIIAL TAKAMQNDRQ KCIEAGANDY IPKPVDVERL FSLMRVWLSK
//
