ID A3XQ51_LEEBM Unreviewed; 384 AA.
AC A3XQ51;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MED217_00960 {ECO:0000313|EMBL:EAQ48324.1};
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:EAQ48324.1, ECO:0000313|Proteomes:UP000001601};
RN [1] {ECO:0000313|EMBL:EAQ48324.1, ECO:0000313|Proteomes:UP000001601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED217 {ECO:0000313|EMBL:EAQ48324.1,
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:EAQ48324.1}.
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DR EMBL; AANC01000009; EAQ48324.1; -; Genomic_DNA.
DR RefSeq; WP_009778587.1; NZ_CH672395.1.
DR AlphaFoldDB; A3XQ51; -.
DR STRING; 398720.MED217_00960; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_039822_0_0_10; -.
DR OrthoDB; 9815750at2; -.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 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; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EAQ48324.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001601};
KW Transferase {ECO:0000313|EMBL:EAQ48324.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 181..383
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 384 AA; 44124 MW; 6D68DB363232A6BD CRC64;
MNFNKDQRFI RWFIIFAAVV ITALILWNVS LFFDQLKQSE RDRMEIWATS MEAFNTEDIN
QYYALSQKIN SKNQYIPIII TDYKDSIVNS INIPENILEN PARSQELLLE MAAENDPIRI
DILGGELWYA YYGHSPVINQ LKFFPVVLVI IVILFIAVIY FFYATSKASE QNSLWAGMAK
ETAHQIGTPL SSLVGWTEIL KAEHVNPDYI EEINKDINRL EIITGRFSQI GSIPKLDPKN
IITETQDAFE YLANRSSKLI DFEIDVPRGQ LFVMLNKELY AWSIENLVKN AIDAMKGKGK
LTLTIKRDTR YAKILISDTG KGIPKMNFNT IFEPGYTTKK RGWGLGLSLT KRIIEEYHDG
QVRVLQSELN KGTTFQIALK LIDE
//
