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Database: UniProt
Entry: A0A0S8CFP7_9BACT
LinkDB: A0A0S8CFP7_9BACT
Original site: A0A0S8CFP7_9BACT 
ID   A0A0S8CFP7_9BACT        Unreviewed;       593 AA.
AC   A0A0S8CFP7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AMK69_19065 {ECO:0000313|EMBL:KPK22805.1};
OS   Nitrospira bacterium SG8_3.
OC   Bacteria; Nitrospirota; Nitrospiria.
OX   NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK22805.1, ECO:0000313|Proteomes:UP000051394};
RN   [1] {ECO:0000313|EMBL:KPK22805.1, ECO:0000313|Proteomes:UP000051394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_3 {ECO:0000313|EMBL:KPK22805.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK22805.1}.
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DR   EMBL; LJNR01000398; KPK22805.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8CFP7; -.
DR   PATRIC; fig|1704023.3.peg.2621; -.
DR   Proteomes; UP000051394; 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; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR031967; PhoR_single_Cache-like_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF16736; sCache_like; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 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:KPK22805.1};
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        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          192..244
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          249..304
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          373..592
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          229..256
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   593 AA;  65959 MW;  9E8B387BC9F12AFE CRC64;
     MAKKKRLLWQ LYPTYILIIV ISLLAATWFA SKTLKQFYHE QSASDLEARA LLFKSQVLEY
     ISPLDTQAID RLCKKAGGKA TTRITVILPS GKVIGDSERD PAKMDNHVDR PEVIQALRDQ
     VGVSTRYSRT LEKEMMYVGI PLKKNSRIVG LVRTSVPLTP MDQALKNIEV KIAVGGLLIA
     VLAAILSLVV SRRISRPIEE IRKGAECFAQ GDFECRLPVS NSEELGSLSE TMNQMAIELQ
     ERINSMREQR SELEAVLSSM VEGVIALDKE ERVISINQAA AQMFETNPSS AQGRSIQEVV
     RNSDLQNFVR NALSSEGPVE CDIVLYSDGE RVLNGHSTVL HDAGGNRRGA LIVLNDVTRL
     RRLENIRRDF VANVSHEIKT PITAIKGFVE TLRDAAMTNG KDADRFLGII QKHVDRLDAI
     IEDLLSLSRI EEDVETEEIV LEEGRIRDVL LTAIQVCQVK AAPKNIRVEL SCSEDLKAKI
     NPPLLEQAVV NLLDNAIKYS GAESEVQVEA KKIDREILIN VRDQGCGIDK KHLSRLFERF
     YRVDKARSRK MGGTGLGLAI VKHITQAHGG HVTVESTPDR GSTFSLHLPP NLN
//
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