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Database: UniProt
Entry: A0A0C1L5H7_9BACT
LinkDB: A0A0C1L5H7_9BACT
Original site: A0A0C1L5H7_9BACT 
ID   A0A0C1L5H7_9BACT        Unreviewed;      1043 AA.
AC   A0A0C1L5H7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=OI18_06840 {ECO:0000313|EMBL:KIC95382.1};
OS   Flavihumibacter solisilvae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavihumibacter.
OX   NCBI_TaxID=1349421 {ECO:0000313|EMBL:KIC95382.1, ECO:0000313|Proteomes:UP000031408};
RN   [1] {ECO:0000313|EMBL:KIC95382.1, ECO:0000313|Proteomes:UP000031408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-3 {ECO:0000313|EMBL:KIC95382.1,
RC   ECO:0000313|Proteomes:UP000031408};
RA   Zhou G., Li M., Wang G.;
RT   "Genome sequence of Flavihumibacter solisilvae 3-3.";
RL   Submitted (NOV-2014) 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   -!- 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:KIC95382.1}.
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DR   EMBL; JSVC01000007; KIC95382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1L5H7; -.
DR   STRING; 1349421.OI18_06840; -.
DR   Proteomes; UP000031408; 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; 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   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR013783; Ig-like_fold.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF07494; Reg_prop; 6.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031408};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        764..786
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          811..1027
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1043 AA;  118283 MW;  63E50A26CEB6C680 CRC64;
     MLLLLIILTT SPTFSQPYYF RHYQVEEGLS NNTVFCSVQG RNGFMWFGTK NGLNRFDGYQ
     FKQFTIADNN QGSGNSDMIY CLSTDMNGAL WVGSAMGLYR FDEKREKLVS FIDSLKEVNT
     VLHDAKGRLW FISWNTVYRY DFGNSELVSY QNLIRATSIC RASNNTLWFG STDGKLYRYN
     ESQNNFSAFE LFSHSPAPPS RWIQKVRCTD DGSILIGTSG QGLKLFDTAK LQYTDLLTEN
     PNRTPIFIRD ILLYDRNEYW LATESGIFIL HRDKAGYTNL RKKFLDPYSL SDNAVYTLSK
     DSEGGVWAGT YFGGINYFSK QHTFFTKYYP DYSSNTVGGS AVREICEDHN GVLWIGTEDA
     GLNSLDKRTG AITHYEPGTS PGSISHSNIH GLLVSGNELW IGTFENGLDI MDLGTRKVVR
     RYKAGSGEHE LKSNFVVSLL ETRSGNKYVG TSNGLFRFTS AGSKFDCPDN FPAGGFISCL
     LEDSKGLVWI GTHGRGIYGY EPSTRKFTNF TFTTGDSLGF PNNIVNAIYE DSKNRLWFAT
     EGGGLCSYNE KQNNFTTYTT KDGLPSNFIF KIIEDDNGYL WVSTSKGLVR FLPEQKSIVV
     FTKANGLLND QFNYNSGYKD ADGNIYFGSI KGMVSFRPGT FHASNFVPQI FITGFQVHNR
     ELSISADSGF LPQSILYTKS LKLPYDQSSF SIDFAALSFT SPEVTAYSYK MDGLEKEWTF
     LKTNRKVYFT NLSSGNYVFR VKAFTNGNWN SKEKKLYIEI LPPFWASTTA YIVYALLVAV
     IAWLLIRRYH RRTQEKKEKE IYEAKIDFFT NVAHEIRTPL TLIKGPVENL LEKTDEIPEI
     REDVTMMNRN TNRLVTLITQ ILDFRKTETR GFSLDFAKED IAPILEESYI TFRPVADKKK
     LNYSLHLPDQ RFTAMADEEA LTKIFSNLLG NATKYASHYV SVILNPPGSD DMYWSLTIEN
     DGPLIPAAMR EKIFEPFVRI KDATRQRGTG IGLALAKSLA TLHGGELLFR EAENGMNLFI
     LRLPVHPPEK EISQKPKRTS QTR
//
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