ID A0A1H1NKU5_9FLAO Unreviewed; 662 AA.
AC A0A1H1NKU5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216503_1635 {ECO:0000313|EMBL:SDR99612.1};
OS Polaribacter sp. KT25b.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1855336 {ECO:0000313|EMBL:SDR99612.1, ECO:0000313|Proteomes:UP000199117};
RN [1] {ECO:0000313|Proteomes:UP000199117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT25b {ECO:0000313|Proteomes:UP000199117};
RA Varghese N., Submissions S.;
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};
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DR EMBL; LT629752; SDR99612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1NKU5; -.
DR STRING; 1855336.SAMN05216503_1635; -.
DR Proteomes; UP000199117; Chromosome i.
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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR008979; Galactose-bd-like_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 PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SDR99612.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199117};
KW Transferase {ECO:0000313|EMBL:SDR99612.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 452..662
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 415..445
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 662 AA; 76839 MW; 45B8E3EA6DB13A25 CRC64;
MRFISCFILL FFLQYSFAFK LIEEKTNIID LRDTQINDDS EIYLDTNWEF YWNDLIIPGN
FNNYKPFKIV TLKDWTEFNL PKTDRSPSFG YATYRLNFRI NKNRPHVSLY IPSAYSSSRI
WINGHFFSEM GHVGKTRSKT IHRRFSQIIP LNTDENNFEI VIQVANYYHN KGGLDKPLIL
GASNHLHDLK SKRIMADMIF IGCLGFIGVF FLFFYLIYWN KDKAILYFAI LCISLSYISL
SDRYAPFTVI FDSISFILLT KFEYITLFLA GASGSLFFNN IFYNFIYRAY SKIIVFSFLA
LVILIFSLSP PHFTKLLIPF LILMIINLIY VTLVVIKAII AKRLESILLL LSIILGSIIF
YIHVFFFLGE NGNAIIYVNF GYILVFLLLS MLLMKRFSDS FQELEHSKEI ALQQKKEIST
QSNQLSRANL ELEENLKLLE NYNAELDDFN HIVSHDLKTP LVSVHALVSF IEEDLKTTLH
ADTKNHINLL KDVVARMDAL INGLLEYSKV AKGNKQKEWF KLNDLLHKVI GVVDNQQKNT
IHLPDEDLEI YANKIELNHV FQNLLSNSIK YNDKKHTIIH ISVVKQNNEY IFSVSDNGPG
IDPKYHNKIF KMFSQLDVNE DVKSTGIGLA IVKKIISENY GIISIESEKG MGIKMNFSWR
IK
//
