ID A6Q215_NITSB Unreviewed; 436 AA.
AC A6Q215;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=NIS_0410 {ECO:0000313|EMBL:BAF69524.1};
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor.
OX NCBI_TaxID=387092 {ECO:0000313|EMBL:BAF69524.1, ECO:0000313|Proteomes:UP000001118};
RN [1] {ECO:0000313|EMBL:BAF69524.1, ECO:0000313|Proteomes:UP000001118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2 {ECO:0000313|EMBL:BAF69524.1,
RC ECO:0000313|Proteomes:UP000001118};
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF69524.1; -; Genomic_DNA.
DR RefSeq; WP_012081787.1; NC_009662.1.
DR AlphaFoldDB; A6Q215; -.
DR STRING; 387092.NIS_0410; -.
DR KEGG; nis:NIS_0410; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_668634_0_0_7; -.
DR InParanoid; A6Q215; -.
DR OrthoDB; 9762826at2; -.
DR Proteomes; UP000001118; 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; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 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, ECO:0000313|EMBL:BAF69524.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001118};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 221..431
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 436 AA; 49754 MW; 6763D4D01868EA65 CRC64;
MLSSQSLKTK LLIRLVIASA ILIALFSTII YKAVQNSLYE EIQEQLIKQA NYIKTNAPNF
HQGQKIDSSY LQKTLNISVE VVSKPKSSKD EIFIQKVVDR KQNKTWMILY YPYDFQEQTY
LKISKDITSI QFILKKLYRI IIFTNILAFA FIIVYAALLS NYLTKYIMKL TAKLSSMNEN
LLKPIKVKDL PMEFQPLGRS INMLINRVQT FVKYQKELFI GIAHELKTPL AVMKLKNEVT
LIKKRSPEEY IQTIKLNIKT INEMNKMIEN VLKIGRQESD QFEPPIEIDL IEYLKEKANN
YQLLARNEDK EIQMDLKPKS YKATIQPTLL NHIIQNFVQN AIKFTPEGGT ITLRSYPVSG
GIKIEVLDEG PGVDESIDLF APFKRIGNKS GVGLGLFLAR SAADAMGAKI EIRNRKDAKG
AVASLFIPTQ LACPIC
//
