ID S2EP70_9ARCH Unreviewed; 497 AA.
AC S2EP70;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BG20_I2003 {ECO:0000313|EMBL:EPA06257.1};
OS Candidatus Nitrosarchaeum limnium BG20.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosarchaeum.
OX NCBI_TaxID=859192 {ECO:0000313|EMBL:EPA06257.1, ECO:0000313|Proteomes:UP000014065};
RN [1] {ECO:0000313|EMBL:EPA06257.1, ECO:0000313|Proteomes:UP000014065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BG20 {ECO:0000313|EMBL:EPA06257.1,
RC ECO:0000313|Proteomes:UP000014065};
RX PubMed=22461554; DOI=10.1128/JB.00007-12;
RA Mosier A.C., Allen E.E., Kim M., Ferriera S., Francis C.A.;
RT "Genome Sequence of "Candidatus Nitrosoarchaeum limnia" BG20, a Low-
RT Salinity Ammonia-Oxidizing Archaeon from the San Francisco Bay Estuary.";
RL J. Bacteriol. 194:2119-2120(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};
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:EPA06257.1}.
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DR EMBL; AHJG01000084; EPA06257.1; -; Genomic_DNA.
DR AlphaFoldDB; S2EP70; -.
DR PATRIC; fig|859192.6.peg.555; -.
DR Proteomes; UP000014065; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPA06257.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000014065};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 182..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..257
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 274..475
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 478..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 238..265
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 497 AA; 55635 MW; FB1006514F977C18 CRC64;
MIGGISAISI INTKYVQETF SSINTETLPI LNTLKNMRYA STHLSALTNE IILIEDETRN
ASENEFAALE ETLETNFYKI EEAKLLFNES FSEYSDIVSK SYPQDVDQIE LVAEKWNEML
FISNKMIQLK TSGASGGTIL NLNNDFDFSY VEMNMAIDKA IELTTANIDQ REIYVESLLR
NVTWSIIIAL NLFVATTLII RFYILRSISK PLNKIKSVTR DIAKGNFVLY PEKGNDEISE
LGKDINIMSK DLKELNKKMI DQERMTSIGG LAIRLAHDIR NPLSVIQNGF EIIKLKTKNN
SDPSLNSNFE SISRSVARIT HQIDDVLNFI NISELHNSKN SLSSILKSTL QSMLIPENVK
IILSENDSTI LCDSSKLNIV FKNLIDNACY AINGNGEIRI RIIESQDDVL VEIEDSGSGV
PDSILEKIFE PLFTTKQVGT GLGLSSCKSI VEAHGGKISV RNNPTTFTIR LPKNLQKTEE
STINNSPNSM IESISYS
//
