ID A0A1H4LIY3_9BACL Unreviewed; 600 AA.
AC A0A1H4LIY3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05443246_1621 {ECO:0000313|EMBL:SEB70225.1};
OS Paenibacillus sp. GP183.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1882751 {ECO:0000313|EMBL:SEB70225.1, ECO:0000313|Proteomes:UP000199177};
RN [1] {ECO:0000313|EMBL:SEB70225.1, ECO:0000313|Proteomes:UP000199177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP183 {ECO:0000313|EMBL:SEB70225.1,
RC ECO:0000313|Proteomes:UP000199177};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNSW01000001; SEB70225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4LIY3; -.
DR STRING; 1882751.SAMN05443246_1621; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000199177; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 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; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SEB70225.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199177};
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};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 331..383
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 490..597
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 600 AA; 67800 MW; 808B5E71DC7ED7A8 CRC64;
MPFPNWLNPN NWFNNWLIRY KIILVYVPLI FVPLFILGLS SNRIYLDAVV QKTIKNVSDN
SSLIITRISG MLTNVESCAN MLTINLNKVI VEDRQTPVSP LEVDLQLYTQ ITNQLSFALL
VFPDVKSAAF IDTSNRVYGS NLAMEVNADL AVNSEVLRQI DASTGNNVWF PMQRRSYLTL
DPKDPVLTLG KKVVNINTGQ KLGIVILNIK ESALSTIYQK IGSIQTGSYF IADEQGVMIS
AQNSQDVLTE IQDPMLKDWV LTENVASDIK SFQDGKKLVV SSQVPNFGWK LISMAPFDAL
TADTRKITML ISLIGLVCLI FAVLGAGILS QVIAKPIIEL TKHMKRVKEG NLDMELEIRS
GDEIGMLASG FNTMIRRIQE LLVNINLEQR KKREYELALI QAQIKPHFLY NTLDVIYTLS
ELGRARDVQR TTKALADFYR VALSKGKETI SLKDEVLNVK DYLSIQRIRY SDVFDFEIDI
ENEILPCTIL KLTIQPLVEN AIYHGLKKKG SFGHLKISGK REERKMILKV IDDGVGMSLE
RQKAVMFGKD ENEEPVGYGL RNVHERIKLY FGEEYGLHID SEPGQGTQVT LQLPFEREES
//
