ID B3Y152_ECO11 Unreviewed; 496 AA.
AC B3Y152;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=yfhk {ECO:0000313|EMBL:BAG66676.1};
OS Escherichia coli O111:H-.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=168927 {ECO:0000313|EMBL:BAG66676.1};
RN [1] {ECO:0000313|EMBL:BAG66676.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B171-8 {ECO:0000313|EMBL:BAG66676.1};
RX PubMed=18757547; DOI=10.1128/JB.00625-08;
RA Ogura Y., Abe H., Katsura K., Kurokawa K., Asadulghani M., Iguchi A.,
RA Ooka T., Nakayama K., Yamashita A., Hattori M., Tobe T., Hayashi T.;
RT "Systematic identification and sequence analysis of the genomic islands of
RT the enteropathogenic Escherichia coli strain B171-8 by the combined use of
RT whole-genome PCR scanning and fosmid mapping.";
RL J. Bacteriol. 190:6948-6960(2008).
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}.
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DR EMBL; AB426059; BAG66676.1; -; Genomic_DNA.
DR AlphaFoldDB; B3Y152; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 277..493
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 496 AA; 55650 MW; AF15EDCBF9C70B36 CRC64;
MLYLNFPSVS IRLFASDESN TLKRWPVFPR SLRQLVMLAF LLILLPLLVL AWQAWQSLNA
LSDQAALVNR TTLIDARRSE AMTNAALEME RSYRQYCVLD DPTLAKVYQS QRKRYSEMLD
AHAGVLPDDK LYQALRQDLN NLAQLQCNNS GPDAAAAARL EAFASANTEM VQATRTVVFS
RGQQLQREIA ERGQYFGWQS LVLFLVSLVM VLLFTRMIIG PVKNIERMIN RLGEGRSLGN
SVSFSGPSEL RSVGQRILWL SERLSWLESQ RHQFLRHLSH ELKTPLASMR EGTELLADQV
VGPLTPEQKE VVSILDSSSR NLQKLIEQLL DYNRKQADSA VELENVELAP LVETVVSAHS
LPARAKMMHT DVDLKATACL AEPMLLMSVL DNLYSNAVHY GAESGNICLR SSSHGARVYI
DVINTGTPIP QEERAMIFEP FFQGSHQRKG AVKGSGLGLS IARDCIRRMQ GELYLVDESG
QDVCFRIELP SSKNTK
//
