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Database: UniProt
Entry: F3LGU4_9GAMM
LinkDB: F3LGU4_9GAMM
Original site: F3LGU4_9GAMM 
ID   F3LGU4_9GAMM            Unreviewed;       719 AA.
AC   F3LGU4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=IMCC1989_587 {ECO:0000313|EMBL:EGG93891.1};
OS   gamma proteobacterium IMCC1989.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX   NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG93891.1, ECO:0000313|Proteomes:UP000010300};
RN   [1] {ECO:0000313|EMBL:EGG93891.1, ECO:0000313|Proteomes:UP000010300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG93891.1,
RC   ECO:0000313|Proteomes:UP000010300};
RX   PubMed=21602334; DOI=10.1128/JB.05202-11;
RA   Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.;
RT   "Genome sequence of strain IMCC1989, a novel member of the marine
RT   gammaproteobacteria.";
RL   J. Bacteriol. 193:3672-3673(2011).
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:EGG93891.1}.
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DR   EMBL; AEVK01000142; EGG93891.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3LGU4; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000010300; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProt.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EGG93891.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010300};
KW   Transferase {ECO:0000313|EMBL:EGG93891.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          389..490
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          564..702
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   MOD_RES         433
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   719 AA;  80978 MW;  07986CC30F2C500A CRC64;
     MWRSLFGKYK EIVAAIAVFL VLDAGVLLLN FYTSYQIADD ARAMHLANRQ SMLTQRIFHS
     VELIHDDLNA GRDIEKNQQK LSISYKQFDE VLDAFIYGGS LIGEGQGQDS LLLDDSYQAL
     SDQYLTVAET LWQPYRNLVG DLVYADYSET LERDKLIEKS LRAMDYSREK GDELLAAVSE
     FAVAVESKAH QKTINLRMVQ GIAIVLAVIN FFIILFHFLK RLRTSDQKAK RSQDEMSEIM
     RTVRDGLFLL TPQYEIGSQY STSMKYLFRQ EDFSSVGFFD LLSPLISDDD LLVAKDYVDS
     LFNPRVKSSL MDELNPLQEV RLNLTNKHGS SDHFFEFTFS RVFEKEKIIH LMVSVKDITE
     NVELRRKLAV SNSKINQEAE SIISLINVDS QLLADFIQLL EEGVKSINEE LEKRVYSSPS
     FVAKLDKINR IAHALKGEAS MLNLTMVEKN LHALEDKLVV LNGKKNLEGD DFLPITVELT
     AIAKSADSIR LFMSRFSEMA MSRDNSHPAP ISSKVKPESA LGRALTQLVN KISRDNKKTV
     LLDLSLFDES LIPAENLNVV KNIIIQLLRN AIIHGLEKPA KRVQRGKPEQ GVISIVVKEV
     AGAITVIVKD DGRGIDFPSI KKHLLMQQVY SQAQVEKMTP RELVKVIFKP GYSTAKKVNN
     HAGRGVGLDV VKTYIDSMGA SLSVGCKAKR SSEFRITIPL QNVDGIDSTR SFDQTDQCA
//
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