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Database: UniProt
Entry: A0A2R5F9T4_9PROT
LinkDB: A0A2R5F9T4_9PROT
Original site: A0A2R5F9T4_9PROT 
ID   A0A2R5F9T4_9PROT        Unreviewed;       568 AA.
AC   A0A2R5F9T4;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NMK_2558 {ECO:0000313|EMBL:GBG14957.1};
OS   Novimethylophilus kurashikiensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Novimethylophilus.
OX   NCBI_TaxID=1825523 {ECO:0000313|EMBL:GBG14957.1, ECO:0000313|Proteomes:UP000245081};
RN   [1] {ECO:0000313|EMBL:GBG14957.1, ECO:0000313|Proteomes:UP000245081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=La2-4 {ECO:0000313|EMBL:GBG14957.1,
RC   ECO:0000313|Proteomes:UP000245081};
RX   PubMed=29411502; DOI=10.1111/1462-2920.14062;
RA   Lv H., Sahin N., Tani A.;
RT   "Isolation and genomic characterization of Novimethylophilus kurashikiensis
RT   gen. nov. sp. nov., a new lanthanide-dependent methylotrophic species of
RT   Methylophilaceae.";
RL   Environ. Microbiol. 20:1204-1223(2018).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GBG14957.1}.
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DR   EMBL; BDOQ01000013; GBG14957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R5F9T4; -.
DR   OrthoDB; 9813412at2; -.
DR   Proteomes; UP000245081; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS 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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF00989; PAS; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GBG14957.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245081};
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        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          172..224
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          225..295
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          298..351
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          372..568
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          336..368
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   568 AA;  63373 MW;  1411B7CFE317F4FC CRC64;
     MSLRFRLNLL ITVLLLIFMA GVGFVILKDT RTSIKEGVEA AGRVTTQLLD TVIVSSYRNP
     ELGPTHEVLK TFLESLGHVR SLDISLYDGS SHLIYLSPPS TYRTDEEPPA WFVKLVAPEQ
     EVSVRRIRFG QLVLTSNPGG AIREAWTGVR NLFMIWLGFF VLLNSVVYWM LGRALTPVNS
     ILRAINRMEH GDLAVRLPGF PLPEYNRIAQ SFNNMAASLE ASTMESRRLA LVVKQTGDAI
     MIHDLNGNIS LWNPAAERMF GYAAEDIIGK SAELLTPPGR ENELRQNLAA IAERRPIYNY
     DTQRVTRSGR LLDVALSAAP LIDPQHNKVV GEICTLRDIT ERKHAEEAER KLEENRQLTQ
     LIQSHIEEER RSLARELHDE LGQYVTAIKT FAVAISNKAK AQMPEIEGAA QTIAAAANHI
     YDGMHNIIRQ LRPGALDNLG LTETLRDAVT NWQGQYPEIE FDLAFSGKLG ELGEMLNINL
     YRIVQESVTN ALRYSQATQV SIQLARLASG EVELTVCDNG VGMNICNVDQ TQHFGLLGMR
     ERVQSLRGTF EVESELGKGV KIKVVIPV
//
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