ID K0B9A0_9ARCH Unreviewed; 370 AA.
AC K0B9A0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NSED_04820 {ECO:0000313|EMBL:AFS82768.1};
OS Candidatus Nitrosopumilus sediminis.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=1229909 {ECO:0000313|EMBL:AFS82768.1, ECO:0000313|Proteomes:UP000006100};
RN [1] {ECO:0000313|EMBL:AFS82768.1, ECO:0000313|Proteomes:UP000006100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR2 {ECO:0000313|EMBL:AFS82768.1,
RC ECO:0000313|Proteomes:UP000006100};
RX PubMed=23209211; DOI=10.1128/JB.01869-12;
RA Park S.J., Kim J.G., Jung M.Y., Kim S.J., Cha I.T., Ghai R.,
RA Martin-Cuadrado A.B., Rodriguez-Valera F., Rhee S.K.;
RT "Draft Genome Sequence of an Ammonia-Oxidizing Archaeon, "Candidatus
RT Nitrosopumilus sediminis" AR2, from Svalbard in the Arctic Circle.";
RL J. Bacteriol. 194:6948-6949(2012).
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; CP003843; AFS82768.1; -; Genomic_DNA.
DR AlphaFoldDB; K0B9A0; -.
DR STRING; 1229909.NSED_04820; -.
DR KEGG; nir:NSED_04820; -.
DR PATRIC; fig|1229909.8.peg.1049; -.
DR eggNOG; arCOG02358; Archaea.
DR eggNOG; arCOG02362; Archaea.
DR HOGENOM; CLU_000445_89_3_2; -.
DR OrthoDB; 342253at2157; -.
DR Proteomes; UP000006100; 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; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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; 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; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFS82768.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..113
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 135..355
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 370 AA; 41845 MW; FFE770B98DAE01BD CRC64;
MLSIKITLFL VSGVSSFIIF YMGIVNFLTS VEETTGLIML IFSIFVATGT LLATVNISRN
ITQPIEKLTQ DMKQFSATNK ASKRTPLKTN VSEIFQLNED FKIMEQRVEK TIELTNDYVE
KLKEMDRKKI EFSSMVSHEL KTPLVPILGY VQMLQKKNFL GELNEKQSDA VNEIHAATIR
LQRLVGDILT TQKLDLGKLD FNKEETNVLE LLNSVIKEFQ PIAEEKKVIL EMNFNEDICI
FTDKDRISQV FSNLIKNSID FVPKSRGIIT IGAKDCGDFV EFLVRDNGSG MSIENQKDIF
KKFYQIDTST SRKRSGSGLG LAICKGIVEG LGGKIWVESK VNEQTTFYFT IPKKPIDSSA
KNELNNKISN
//