ID A0A1I1P653_9GAMM Unreviewed; 1778 AA.
AC A0A1I1P653;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05660831_00500 {ECO:0000313|EMBL:SFD02473.1};
OS Thiohalospira halophila DSM 15071.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalospirales;
OC Thiohalospiraceae; Thiohalospira.
OX NCBI_TaxID=1123397 {ECO:0000313|EMBL:SFD02473.1, ECO:0000313|Proteomes:UP000198611};
RN [1] {ECO:0000313|EMBL:SFD02473.1, ECO:0000313|Proteomes:UP000198611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL3 {ECO:0000313|EMBL:SFD02473.1,
RC ECO:0000313|Proteomes:UP000198611};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOMJ01000001; SFD02473.1; -; Genomic_DNA.
DR STRING; 1123397.SAMN05660831_00500; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000198611; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd02205; CBS_pair_SF; 2.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 5.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 6.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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; IPR036641; HPT_dom_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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00571; CBS; 4.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 3.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 4.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 6.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198611};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 135..192
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 200..257
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 275..319
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 435..483
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 487..539
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 540..612
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 616..669
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 743..793
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 868..919
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1063..1286
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1303..1428
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1449..1563
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1608..1700
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 258..285
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1033..1063
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1357
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1498
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1647
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1778 AA; 199375 MW; 537CA84BCDBCAF92 CRC64;
MFFPEIRTIA TTDVVTVPPT ATIADAVRTM KDHDIRDVVV RDTEGYRLFL SSTLLELESR
GLDFRTPLEQ LDLPRPATLP PDASVLDGLK AIRNRSDHIC LVGPADELSG ILSYSDLAGS
LDPRTLAQTQ SLGELLRGIH ALELDPAESL HSAMTGMADQ GHDAAIIVED GRPSGLLTQR
DIVHLLDSRT DPATPVGDCM TRPPQTLHEQ ASIAEALEFC RERHIKRVVV VDDTDRLTGV
ISQKELVNLY YNQWFTLLKD HQAELGRLNE ELQEKNRALE SLTEEVPDGL LALDADGTVT
RASRAAADML DTEPARLIGL PVFNLFRCAD QSAEAGRQDG EFTEQPISPG DCRVHQALRA
RTPYRGREML SRGDGQQRVV DIRTKPLADD GSAILLFHDV TAEERAEAGR RQEQEFFSGG
PVVVFVWRPE PGWPVHYVSP NVEQVLGYSV NEVMAPDFRF IDLVHPDDVE RLGDEVTAAL
ARGDTAFEQY YRLQTRAGEC RWFYDYTAPE YDEAGRPRLI RGYILDRTEE RQARERLAEN
EERWRFVLEA TDQGVWDWDA TTDSVYFSPQ WKRMLGLEEH EVGNDLDEWK SRVHPDDLDN
VLADLERHFR GETDTYENEH RVRCKDGSYK WILDRGRVIK RDGDGQPLRV IGSHTDMTER
HALVESLEEQ QNRFRTLFEL YPDATLIIDP ESGLPVQFNR LAHEQLGYTA GEFAELRIPD
YEAQETPEEI ADHIRTIFKF GRDDFETRHR CKDGSIIDVR VSVILLHLEG RTLFLAVFRD
ITEQEQNRQQ LAAEEAKFRG LFELSPVGIA MNDFATGEFL DFNDAVNEPA GYTRQEFAAL
SYWDVTPREY MPLEMAQLES LQRTGRYGPF EKEYIHKDGH RYPVLLHGFK TTTPEGREVI
WSLIQDISEQ KATEQALRET TERFGGIFEQ TSSGVAVYRP VDDGEDFVFV DYNPAAEQMD
QTERDTVLGH RLTACFPGVR DIGLLAAFQR VYRTGEPEHL PVSEYRDNNI VGWRENRVFR
LSSGEVVAVY DDLTKVKQAQ QESERAREEA ERASRAKSEF LANMSHEIRT PMNAVIGLSQ
LLEQTDLGEK QRDQVNKIHQ SSRMLLGIIN DILDFSKIES GRLELEVRDF ELNEVVDQMA
TLFGEKAHND GLELIYDIQP DLPRSLVGDS LRLSQVLSNL LSNAIKFTDQ GGTVELGVRA
VERPDAERIT LRFHVRDTGI GMSQVQRARL FRPFSQADSS TTRRYGGTGL GLVISRRLVE
KMGGTLEVDS APGEGSTFTF TLTLPLGEDQ RSSVDCPDTT GHRVLIVDDQ DSAREVIRTL
LDHCGFSTEE ATSGEAAIRQ VVAAEQRGAP FDFILMDWWM PGGMDGSETC EEIERLRQRG
ELEETRPPIL MVSAYSQDEI DLPDGLTIDY MAKPITASSL YDALVRAEGG TVTTRPPTSG
EVPNLNGRHL LLVEDNEVNQ EVATLLLERT GARVVTAENG GEALEQVRSE APDLILMDLQ
MPVMDGFEAT RTLRDEGFNG PIIALSAAVM DDDREHARAA GVDDHLGKPI ESEDLYTALS
NHLAPIATHR AEPPSARELR GESGAIAGLP EELPGFDIPR GRQLLGGDDA LYARLLRSFR
GKLASDYAPL LDHLRAGRDE EARRIAHTLK GAAGTLGATT IQWLAEEIDS TLKAGHPVTE
DDISRLEQAF QEADRALEAL SPSGTAGSAG TRAAVETLRQ RLTNSELVEE ETLREATGYL
RGRGLECDEL ESKVEQMDFD EALQHLDELM DTDDDGDT
//
