ID A0A090AJQ2_9GAMM Unreviewed; 824 AA.
AC A0A090AJQ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=THII_3417 {ECO:0000313|EMBL:BAP57714.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP57714.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP57714.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
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; AP014633; BAP57714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090AJQ2; -.
DR STRING; 40754.THII_3417; -.
DR KEGG; tig:THII_3417; -.
DR HOGENOM; CLU_343533_0_0_6; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000031623; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 2.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAP57714.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000031623};
KW Transferase {ECO:0000313|EMBL:BAP57714.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 265..335
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 338..390
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 430..474
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 635..687
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 688..731
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT COILED 396..433
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 824 AA; 94660 MW; C8FAFF680592711A CRC64;
MLQDDQYSES QMFLTGTSLL VVVTVLLLLI SLIIQHFLPM WQWDQILLHA SLQIVGAFMA
ISLTLLLWVL KKLKSIDSTQ LWIGCALLGM GLLDGLHALV LMGDSLVLLQ SITTSIVGVW
FGLVWLPNRF RYYFCQNKIA FIIVILLSIT LGILSLAFST QMPWIEETET HWYIIPLNTI
GGIGFFLAAW YFFRTPFSSD FGHLLFSSHC FLLGLATVLF QLAHEWNAWD ATWVFWHLLR
LAAFFLLSYY LFSLLNQAVR QLWVNQEHLR LIMEVAPVGI FYVDMQGYDS SINKKGVEIT
GLAAEEAVGK GWIKAVHPDD RKQVLSQWQE AINHNQIFKS QHRFKHPNGT VIWVTAQAVA
ERTADDEIMG YVGTLTDISE TKQTEAQLTR YRNHLEEMVV QRANQLTQAN QQLQQKMEER
QQIEIALRES EARFASILNI APEAIITVDQ LQQIILFNQG AERLFGYTSK QIMGMPLDTL
VPSRLQAKHH QYFTEFTHEP VTVRHLDESL GIFGQRQDGS EFPIEGSVSK LDQQKGTLFI
VILRDAAKRW QSEQVLRENE EFYLLMMGGG KVGIWDWHIN HDRLYISPHF KTLLGLNEPA
ANLQMADWFK HVYPEDLDRL KAAIEQYLQG VIPRYEIEYR VQDPTGHIHW ILMRGHSLRD
QNDKPYRFTG TSTDITELKQ IATTLQETEQ KYHLLLNSAK EAILILDNQG NVLEANTIAE
ILFGYQREEL LQSNISLLYA ASQNACLQDS FTTGTCNLYE APILTKSGQT ILVDIYGSVI
ECGEQKRLLT IIRDIRSRQQ AQMALEERRI LLTHQLEQQT IPNY
//
