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
//