ID A0A1Y6CBD2_9PROT Unreviewed; 942 AA.
AC A0A1Y6CBD2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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=SAMN05428998_12020 {ECO:0000313|EMBL:SMF55133.1};
OS Tistlia consotensis USBA 355.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Fodinicurvataceae; Tistlia.
OX NCBI_TaxID=560819 {ECO:0000313|EMBL:SMF55133.1, ECO:0000313|Proteomes:UP000192917};
RN [1] {ECO:0000313|EMBL:SMF55133.1, ECO:0000313|Proteomes:UP000192917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 355 {ECO:0000313|EMBL:SMF55133.1,
RC ECO:0000313|Proteomes:UP000192917};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWZX01000020; SMF55133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6CBD2; -.
DR STRING; 560819.SAMN05428998_12020; -.
DR Proteomes; UP000192917; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR007890; CHASE2.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01080; CHASE2; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000192917};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 444..495
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 716..937
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 99363 MW; EB045517EF62CFB8 CRC64;
MRRLQRRIRT DSAPGMPAAR AGAFGPEPPP VTPKRSPLVG AALLAILLLA WSADLTPIAA
LRLWGFDLAS SLRPEAAGNP QVAAVEIDDE SLARDGRWPW PRDLLGRVVA RLAEQGAAAV
VLDILLAEPD RLGERDASLA SAMALLPVVS GAAVPASLPL SAERDPIVGR FATRGVPDLA
RLPHASAILR ALPVLEGAAA GVGLVNLYPD LDGATRTVPG AVAVGARLVP GLAIEAVRVA
AGAPNLILEM PTRLGAEGIA IAGHLVPTDA RGRIWIDSRN PDRIPVVAAH RLLSGETPDA
EVAGRVVVLG VSASGIAATL RTASGKGVPS SLFQAMAVDS ILSGTVMERP PVMPLVEAGV
AVALGLAIVA ASPWLSLPLL AALAAGLAAG LAAGAAALAL GTGLLADASF PLLTGLVLTG
QVAVVRLREQ ILIRRQQSAI LARQDAYMRQ VVDASFDAIV TVDAEARILT ANAGAERLFG
VPLRDLPGRR IDELLTGFWA EAMGDQADQR ALGDAARSRQ VIAATAVHSQ GARIPVEMTI
AETEMEQPVF AIVLRDISAR IGAEEAARRA GERLHDGVGR ITDGFALFGP DRRLVVCNAR
FVAMLGEAGA DAAPGVRYDS LMARYARSAG APVDAAARTD AWLSERMEAF STGRPPRIQE
CLDGRWFRID ERPTAEGGLV GVYSDITELK RHEMEMAEAM HRAEAASLAK SEFLANMSHE
LRTPLNAVIG FADLMKRELF GPLGNEHYRS YVADIIESGS KLLAMIESIL EFARSEQKEL
TRPAGQSRLD EVVGAVLRDL HPTALEQRVD LQTDLDDGLP ALAVDASVLY QILQNLVSNA
IKFSKPGTAV RVRTFVDADG GPAMAVKDRG IGIPAELIDR LTQPFWQRQS ALVRSHEGVG
LGLAIVKSHV DNLKGELVFE SRVGEGTTAT VHLPATCLAE PV
//
