ID A0A2U3QE86_9BACT Unreviewed; 830 AA.
AC A0A2U3QE86;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=NBG4_110031 {ECO:0000313|EMBL:SPP99728.1};
OS Candidatus Sulfobium mesophilum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Sulfobium.
OX NCBI_TaxID=2016548 {ECO:0000313|EMBL:SPP99728.1, ECO:0000313|Proteomes:UP000245125};
RN [1] {ECO:0000313|Proteomes:UP000245125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zecchin S.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; OUUY01000013; SPP99728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3QE86; -.
DR Proteomes; UP000245125; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd18773; PDC1_HK_sensor; 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; 3.
DR InterPro; IPR033479; dCache_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; IPR013656; PAS_4.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 2.
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); 2.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245125};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 280..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 303..355
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 431..485
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 486..541
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 564..614
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 625..825
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 830 AA; 93890 MW; EE742675898757B2 CRC64;
MKHRGIRKRI VIAVILLLVI SFTLLGTALS VLIYQKEKEQ FVSLQHEVVS FAANEMLWDI
HELQALLGLA GENYDWARRN GITVAGFLSQ ILMAEHVKHH NIVDELSFFD ETGRERERVS
RLSVYGAADL RDLSRNDEFA VPKKSGEAYF GPVTFEQSTF APYMTMSVPV MDAKRSNIQS
VLMANIRLNK IWQNAVERTI GKTGTIFITD DRGKVLAHPD PSVIFRNTFY TPSSLEGIHR
GLSNTDVMLV GRKVEVGNRI FFVYAAVPFE EVIGLSRDTL FAVAIFFCGF LVFSISLCLV
AVNRIVRPIE TLANNARKIT AGELTATLNI KSSDEIGELS GALNVMTARL MDTIHSLEQR
NELVNNVLNS MTHPFYVIDA NDFTIKMANP AANFSVEMGK TTCYALTHKS GEPCKENEHP
CVIQEIKRTG KTVTVEHVHR GDNGEQHFYE VHGYPIYDKA GNIVQVIEYN FDITERRKIE
DQLRMSEQKN RIITSSAKDA IIMMDEDGRM LFWNPAAETI FGYDEEEMIG RELHSIIVPD
SYRDEYLEGM GKLRENGNGA GAGQTIEIVA KRKNGTEFPV ALSLSAFQLN NRWHAVGIAR
DITQRRLAEK RILDSLEEKG LLLQEIHHRV KNNLQIISSL LDLQLEYVAG RKPQDVFSEI
KNRVKSIALV HEKLYLSKDI SKVDFNDYLL TLIDNLYRSY NISLARIALK LDVEDVFLGI
DTAIPCGLVI NELFTNALKY AFPGERNGEV HVMLRKTGKD EKGVGLYELR VEDNGIGMPH
EVDTRGSKTL GLHLVTTLVE HQLRGSIDLK REGGTKFYIR FKELKYKKRV
//