ID Q5QVC6_IDILO Unreviewed; 577 AA.
AC Q5QVC6;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=IL2120 {ECO:0000313|EMBL:AAV82952.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82952.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV82952.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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};
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DR EMBL; AE017340; AAV82952.1; -; Genomic_DNA.
DR RefSeq; WP_011235348.1; NC_006512.1.
DR AlphaFoldDB; Q5QVC6; -.
DR STRING; 283942.IL2120; -.
DR DNASU; 3172331; -.
DR KEGG; ilo:IL2120; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_133_5_6; -.
DR OrthoDB; 2521613at2; -.
DR Proteomes; UP000001171; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; 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 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, ECO:0000313|EMBL:AAV82952.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001171};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..239
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 344..575
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 220..335
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 577 AA; 64727 MW; 73D28C16E704B777 CRC64;
MAIKSISSSL LTRVLSVYFL LTLIVTAIQI GAEYFDTKRV LIAELQNQQS TFNGSLTRSL
WEFNSNQIDT IADGLISIPA IAGVLIRDDA GNILVQLGET TEMSDLPDDN SEGALLPERN
GIFGYYDSLI FEFSGHSTKV GDVSLFSTRD IAIDRIKVSL GFIIGNAIIK SIFLIVLFTI
AFNRMLNRPL SDLTQQIKGF RLDNLERSRI RLDDQHNNEL VLVEQAYNQL LDNIEEYQSD
LDRTQKKLKA ANRQLDEQNA ILEQEVARKT SSLSQVMLDL EQRKNELEMR QEKLEREVGQ
RRAIENTLRQ SNQRLESSLN NLRETQQQLI ESEKMASLGG LVAGITHDVN TPIGISVTAS
SYLREKLDTL DQSLLNKELT QTQLKKFIEE GRESLNLLDS NLHRASDLIS SFKQVAVDQA
SDAIRDINLK SYIEDLVQSL QPHLKKTNHQ VRLECADDIF IRCPAGALSQ IFTNLILNSL
RHAFDGISEG LMIISIRLDG ETLQVHYSDN GNGLSEAQLK RLFDPFFTTK RDQGGSGLGT
HIVRNLVTQT LSGEISAESE PGKGLSYFFS FSVQVLN
//