ID A0A251X9R0_9GAMM Unreviewed; 999 AA.
AC A0A251X9R0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=TPSD3_08880 {ECO:0000313|EMBL:OUD14413.1};
OS Thioflexithrix psekupsensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thioflexithrix.
OX NCBI_TaxID=1570016 {ECO:0000313|EMBL:OUD14413.1, ECO:0000313|Proteomes:UP000194798};
RN [1] {ECO:0000313|EMBL:OUD14413.1, ECO:0000313|Proteomes:UP000194798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D3 {ECO:0000313|EMBL:OUD14413.1};
RA Fomenkov A., Vincze T., Grabovich M., Anton B.P., Dubinina G., Orlova M.,
RA Belousova E., Roberts R.J.;
RT "Thioflexothrix psekupsii D3 genome sequencing and assembly.";
RL Submitted (DEC-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 -!- 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:OUD14413.1}.
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DR EMBL; MSLT01000012; OUD14413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251X9R0; -.
DR OrthoDB; 9792854at2; -.
DR Proteomes; UP000194798; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
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; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_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; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000194798};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 299..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 319..371
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 539..755
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 779..895
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 505..532
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 828
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 999 AA; 113097 MW; F2311905C66E7602 CRC64;
MKLQYKLPLS FNLIVLLSVL LTSGFAIHYF NKTLEQQAYQ ILDEKADVAW LIYQKQLEHI
GNNAKHIAYD TSLQKSLAEK NFFGIEQLLE RLLKDKHIYH ATLLQLDEQH VTILDIEGHI
VAQIGLENYP LFSYHLSNLD VNNPLLQRAL LERKLLIFPE LIAGSPIVSL SAVMPIVKKE
QIDAFNEKTS LIGLVLLRSV LQNNVELTQQ ISELLGVSSA IYQDARPISS SHSLSPLNEQ
RYAQILQGQL EQTGYFEKGQ LLSRFFPLKD VSGEPIAALG IHLQADQYVD TAHKVIQDLL
WMTLLCLIGT LLLSFVILRS ILHPARQLLE GVNRIHAGEL QHRIVVSAHD ELGLLGKAFN
DMANRLSESF NLLEQRIQNA TEKLHHTLVH QRSIMDTMTD GLLVTDTDNH IVLYNSAFEK
LFPNYPPVLG GHCSEVCSPE LQQLIRQAQN EQIVTTVEII PLSNMRIGNA VAAPIFQAIE
LNTPIPEIAE EYSGLVVLVR DITAQKQVEY ELAEEKNRAE QARAEAEVAN QAKSVFLANM
SHELRTPLNG ILGYAQILLR DPQLTKKQLE GVEIIRRSGD YLLTLINDIL DLSRIEANRI
ELYVTDIIFS DFLNDIVELF KIRAEQKGIA FIYEQLSQLP QGIRGDEKRL RQILINLLGN
AVKFTEQGGI TFKVGYFEKK LRFQIEDTGI GIADEDLEKI FQAFEQAGDQ NYRAQGTGLG
LAITKRLVEM MGGELKVESH LHQGTTFWFC LELPEVSELI PSKMTQIPVI TGYEGTRRHI
LMIDDRWENR SVMHNLLIPL GFSLDEAENG EEGLRKAIEK TPDLIITDLV MPVLDGFEVA
RRARQHPALK HIPIIAASAS VFDYHQQESF AAGCNEFIAK PVRFDILLNA LEKHLNLQWI
YDHRDDLIHL PLLDETVAMS ELDSEESKEL LTPQQATMLH QLILMGDIAG IIDKAESIIA
ESPKATLLMQ RICRYAQQFE DDKIMTLLKS YLDAQQEEK
//
