ID A7MGZ7_CROS8 Unreviewed; 463 AA.
AC A7MGZ7;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=ESA_00706 {ECO:0000313|EMBL:ABU75983.1};
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU75983.1, ECO:0000313|Proteomes:UP000000260};
RN [1] {ECO:0000313|EMBL:ABU75983.1, ECO:0000313|Proteomes:UP000000260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU75983.1,
RC ECO:0000313|Proteomes:UP000000260};
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU75983.1; -; Genomic_DNA.
DR AlphaFoldDB; A7MGZ7; -.
DR KEGG; esa:ESA_00706; -.
DR PATRIC; fig|290339.8.peg.623; -.
DR HOGENOM; CLU_000445_89_23_6; -.
DR Proteomes; UP000000260; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
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; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000260};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..463
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002710993"
FT TRANSMEM 160..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 241..457
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 463 AA; 52075 MW; 931FB5C7DA43D3DF CRC64;
MMAFLLVMVP LLFLAWQAWQ SLNTLSAQAA QSNTLTQMDA RRSEAMTNIA LEMERSYRQY
CVLDDVTLAK VYESQRQRYS RMLEAQASVL PDARLYKALR QSLVDLAQLE CHNSGPKPDA
ATRLEAFADT NTRLVQATRA VIYARGQQLQ QEIASRGRLF GWQALALFLA SLALVLLFTR
MIIGPVKGIE RMINRLGEGK SLGTAMMFKG PRELRSVGQR IIWLSERLAW LESQRHQFLR
HISHELKTPL ASMREGTELL ADQVVGPLTA EQREVVEILD TSSRNLQTLI EQLLDYNRKL
AGGAVELEKV ELAPLVEIVI ASHSLPARAK MMHTEVSLAD APCLAEPMLL MSVLDNLYSN
AVHYGRESGT IYLRSRRLAS TLCIEVANTG TPIPEAERQM IFEPFYQGSH QRKGAVKGSG
LGLSIAQDCI RRMHGELRLV EDDTADVCFR IELPLFDPER LKK
//
