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
//