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Database: UniProt
Entry: D0Z3K9_PHODD
LinkDB: D0Z3K9_PHODD
Original site: D0Z3K9_PHODD 
ID   D0Z3K9_PHODD            Unreviewed;       481 AA.
AC   D0Z3K9;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=VDA_001010 {ECO:0000313|EMBL:EEZ39990.1};
OS   Photobacterium damselae subsp. damselae CIP 102761.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ39990.1, ECO:0000313|Proteomes:UP000003579};
RN   [1] {ECO:0000313|EMBL:EEZ39990.1, ECO:0000313|Proteomes:UP000003579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ39990.1,
RC   ECO:0000313|Proteomes:UP000003579};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA   Bartels D.;
RL   Submitted (NOV-2009) 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; ADBS01000002; EEZ39990.1; -; Genomic_DNA.
DR   RefSeq; WP_005305978.1; NZ_ADBS01000002.1.
DR   AlphaFoldDB; D0Z3K9; -.
DR   eggNOG; COG2205; Bacteria.
DR   Proteomes; UP000003579; 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; cd06225; HAMP; 1.
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; 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; PTHR44936:SF5; SENSOR HISTIDINE KINASE ENVZ; 1.
DR   PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR   Pfam; PF00672; HAMP; 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   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEZ39990.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003579};
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        204..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          223..275
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          283..478
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   481 AA;  54827 MW;  F40BC1FBB20DEC58 CRC64;
     MQLKSIWPKS LLARTLWLTL LAVFFAQLIS TMIWYSQSKQ RDLKGLESTS ASMATMFAST
     VNFFQSLPTE YRHIVLDQLR NMGGTRFFVS FNSEKIRITP IANSELKQAA ISTFETVLHD
     KLPQQDQIKV EFSRPETLHV LKNDILLSDL PKSWAHYTLS LEPLSPPILV VQIQLEHNQW
     LYIAALLPAP YMMLEDQIMT SHQVFSLLFT TLLLLVFTYL MISKQTKPLK RLANAANALS
     LDIYQPPIKE EGASEIVTAT RAFNRMQLRL MRYIDDREKL FSSISHDLKT PITRLRLRAE
     LIDDESKIEK FNRDLDELEM MVKGALQCVR DTDLHENLVT VDVLDILHHI AEGHNSQQRK
     VRILEKPIAP LMAKPLALKR CFTNLIDNGV KYGERVTVLI SDESDALVLI IKDQGKGIPL
     EQQDAVFEPY YRLAKDKDGH GLGMGIARNI VRAHGGDLTI HNANDGGLEV KVFLPRFANN
     Q
//
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