ID Q82XB0_NITEU Unreviewed; 683 AA.
AC Q82XB0;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=NE0377 {ECO:0000313|EMBL:CAD84288.1};
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD84288.1, ECO:0000313|Proteomes:UP000001416};
RN [1] {ECO:0000313|EMBL:CAD84288.1, ECO:0000313|Proteomes:UP000001416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC {ECO:0000313|Proteomes:UP000001416};
RX PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L.,
RA Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., Hommes N.,
RA Whittaker M., Arp D.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD84288.1; -; Genomic_DNA.
DR RefSeq; WP_011111012.1; NC_004757.1.
DR AlphaFoldDB; Q82XB0; -.
DR STRING; 228410.NE0377; -.
DR KEGG; neu:NE0377; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_024784_0_0_4; -.
DR OrthoDB; 9785691at2; -.
DR PhylomeDB; Q82XB0; -.
DR Proteomes; UP000001416; Chromosome.
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; 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; IPR014265; PrsK.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR02916; PEP_his_kin; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CAD84288.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001416};
KW Transferase {ECO:0000313|EMBL:CAD84288.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 479..681
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 484..546
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 683 AA; 77013 MW; 6989E95EB6543ED4 CRC64;
MTTLSYAAAA AAFFFLSILL ITSWRGRLYG LLLAAACLSS SIWAATIAGL SYLDYAYPLL
IQVLELLRNA TLTIFLITLL GPFQPGKTDN TSPKIRPAVA AIALFYLICL AQIVVFGQTT
GIDPDQPGAS RDFLIWVAMA IIGMILVEQY YRNTPREQRW GTKFICLGIG GLFVYDFYLY
SDALLFRKIS ADIWVARGWV NTLIVPLIAL SAARNPKWTV GIAVSRRILF YSSALFGAAV
YLLLMAAAGY YLRFSGGTWG TIFQLTFLFG AIILLIVVLF SGTTRSWLKV FISKHFFSYN
YDYREEWLRF TRTLSEEETE LRVRVIKSLA QLVESPAGGV WFKSEQHHAY LPIARWNIPH
IDASVAIDSY FCQFMQESSW VIDLYQHDSE SQKYAAMILP DWLPTIPKAR WVVPLILHGE
LLGFVVLTEP RSAVEFNWEV RDLLKVAGRQ AASYLAQYEA AQALSTARQF ESFNRMSTFI
VHDIKNLIAQ LSLLLTNAEK HKDNPEFQQD MLDTVALSVN KMKRMLEKLS SENIREEKNA
LSLNELLQRI IASKSFYEPQ PVLDILDTEL NVLADLSRLE RVLGHLVQNA IEATPKDGYV
EVRLKQQPGW AVIEIEDSGH GMSEQFIREK LFTPFESTKT AGMGIGVFES REYVEEIGGK
LHVSSEVSKG TIFTVMLPLV SPP
//