ID A3XH06_LEEBM Unreviewed; 487 AA.
AC A3XH06;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MED217_17875 {ECO:0000313|EMBL:EAQ51436.1};
OS Leeuwenhoekiella blandensis (strain CECT 7118 / CCUG 51940 / KCTC 22103 /
OS MED217) (Flavobacterium sp. (strain MED217)).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Leeuwenhoekiella.
OX NCBI_TaxID=398720 {ECO:0000313|EMBL:EAQ51436.1, ECO:0000313|Proteomes:UP000001601};
RN [1] {ECO:0000313|EMBL:EAQ51436.1, ECO:0000313|Proteomes:UP000001601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED217 {ECO:0000313|EMBL:EAQ51436.1,
RC ECO:0000313|Proteomes:UP000001601};
RX PubMed=17215843; DOI=10.1038/nature05381;
RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA Neutze R., Pedros-Alio C., Pinhassi J.;
RT "Light stimulates growth of proteorhodopsin-containing marine
RT Flavobacteria.";
RL Nature 445:210-213(2007).
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:EAQ51436.1}.
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DR EMBL; AANC01000001; EAQ51436.1; -; Genomic_DNA.
DR RefSeq; WP_009781910.1; NZ_CH672395.1.
DR AlphaFoldDB; A3XH06; -.
DR STRING; 398720.MED217_17875; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_043647_0_0_10; -.
DR OrthoDB; 9776727at2; -.
DR Proteomes; UP000001601; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001601};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..261
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 278..486
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 228..269
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 487 AA; 55930 MW; 2EAABD9848B72048 CRC64;
MKFNKLSLRL RIFFGMVLLI LGASILIGII SVVQYKEEAK EYHRDRLLRK EDQIRAEIDY
VLDQTSYEVI SKNIPFILKF NNDIYRIADV HELPINIYDL DGKLLVKSKE TFTEDTLETS
LNPSVLEGLA NTPTKRWIVQ SEIDGVKYQS SYTYINDNKF KPLAIMNLPY IQDDDFITRE
LDEFLRRLAE GYLFMLLIAT VLSYFLSRYI TRSLKTISDK MIQTRLDKRN QRIEIDDASE
EISNLVRSYN GMIDELENSA AKLAQSEREA AWREMAKQVA HEIKNPLTPM RLTVQSFQMR
FDPNDPDIHK KLDEYSKTLI QQIDTMSSIA EAFSNFAKMP AQQNETLNVV FVTKLALDIF
TEHYLTFGTD AEEITVKLDR TQLIRVVTNL VKNAIQATEG VQDPKIRVEI KSDVDTVCIL
VCDNGHGIPE ENIEKVFEPK FTTKSSGMGL GLAMVKNIVE TYNGTITFTS KEDRGTVFKV
TFPKAEA
//
