ID W7D0T7_9LIST Unreviewed; 609 AA.
AC W7D0T7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PRIP_15654 {ECO:0000313|EMBL:EUJ42680.1};
OS Listeria riparia FSL S10-1204.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265816 {ECO:0000313|EMBL:EUJ42680.1, ECO:0000313|Proteomes:UP000019248};
RN [1] {ECO:0000313|EMBL:EUJ42680.1, ECO:0000313|Proteomes:UP000019248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL S10-1204 {ECO:0000313|EMBL:EUJ42680.1,
RC ECO:0000313|Proteomes:UP000019248};
RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT sp. nov., from agricultural and natural environments.";
RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
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}.
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:EUJ42680.1}.
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DR EMBL; AODL01000034; EUJ42680.1; -; Genomic_DNA.
DR RefSeq; WP_036102089.1; NZ_AODL01000034.1.
DR AlphaFoldDB; W7D0T7; -.
DR PATRIC; fig|1265816.5.peg.3092; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000019248; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; 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; IPR013767; PAS_fold.
DR InterPro; IPR049814; Resp_reg_WalK.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; NF033092; HK_WalK; 1.
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; PF00989; PAS; 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 SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 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:EUJ42680.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW 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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..258
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 263..335
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 385..602
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 609 AA; 69519 MW; 17D7E7519D29B2FD CRC64;
MRRMKFFQSV QFRFVMIYLL LILVAMQVIG AYFVRELQDQ LEKNFKTAIT NSVNLLEYNV
REEMLKYTND DQTKLESDIQ SMLLDFVRGS NDFEEVLVVD NKMKIIGTSD VDNQGIVGQV
STNKMIKNTI NSGNGENKIF MGKNPKRQIW VDVSPITSKG EVIGAIYLAT DIESVYEQVD
SITSIFITGT LLAMAITAIL GILLSRTITK PITDMKRQAF AMARGNYTRK VKVYGMDEIG
QLAESFNALT KRVQEAQAMT EGERRKLSSV LSYMTDGVIA TDRRGKVILI NTPAEKMLKV
AHESANGKPI IDVLDVADEY SFDDLMELDE PLTMDRSTFE DPYVLRANLS VIQRETGFVN
GIIAVLHDIT DQEKVDQERR DFVSNVSHEL RTPLTSMHSY LEALSDGAWR DEEIAPRFLE
VTQSETERMI RLVNDLLKLS RMDSGRTNLE KNFVNFNDFF NHIIDRFEMM KKDGITFKRH
FTREPVIIEI DEDKIMQVMD NIISNANKYS PDGGRITFYL RKREDEIEVS ISDEGMGIPE
EDLTKVFDRF FRVDKARSRE MGGTGLGLAI ARDVIKAHGG EIWAQRNPSK GTTISFTLPY
NDLPEDDWE
//
