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Database: UniProt
Entry: Q5QVC6_IDILO
LinkDB: Q5QVC6_IDILO
Original site: Q5QVC6_IDILO 
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
//
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