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Database: UniProt
Entry: A0A1G6BGH5_9FLAO
LinkDB: A0A1G6BGH5_9FLAO
Original site: A0A1G6BGH5_9FLAO 
ID   A0A1G6BGH5_9FLAO        Unreviewed;      1248 AA.
AC   A0A1G6BGH5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN03097699_0044 {ECO:0000313|EMBL:SDB19705.1};
OS   Flavobacteriaceae bacterium MAR_2010_188.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1250295 {ECO:0000313|EMBL:SDB19705.1, ECO:0000313|Proteomes:UP000199442};
RN   [1] {ECO:0000313|EMBL:SDB19705.1, ECO:0000313|Proteomes:UP000199442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mar_2010_188 {ECO:0000313|EMBL:SDB19705.1,
RC   ECO:0000313|Proteomes:UP000199442};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; LT629302; SDB19705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6BGH5; -.
DR   STRING; 1250295.SAMN03097699_0044; -.
DR   Proteomes; UP000199442; Chromosome i.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; 3.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07494; Reg_prop; 1.
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; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF101898; NHL repeat; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SDB19705.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199442};
KW   Transferase {ECO:0000313|EMBL:SDB19705.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        935..953
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1007..1248
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1248 AA;  141214 MW;  EDD20ADCC978BBFF CRC64;
     MKPIFYSRPL QIYCITVLFL AIFSCNQKER AVPFPENENE YSRPADSPLQ FSEPKKIEWS
     VNDTTNFKAA TVKKVNLENL PSKPFYPDGF LPLNNPIEEI NFDFTTLPDT LINIKELASK
     PIRFKTSIIE PPLSVPAGLP KLKKNASMGI LEFGEDQGLP GYLVTAMMED SYGMMWIGSD
     KGLCRFNGEY IEIYSFIDNI FTGALAEISS MLEDNKGRIW IYTSQKGIYV LDLKAGVVRN
     ANFIKQEFNF NPDCSMVMDS RGFIWLGTIQ DGFYILNPSN ETYRHVSQLQ PQDNGNAKRI
     LEDSSGNIWI SSIAGLSIID YDKGRIRFLN SSEELSMPSA TAFFNDRKNR IWVGTEDNGI
     SILDLEHDKI QNLGSSQGFT NSIQHFTQGN DDKLWMSTAA GVYVFDVEKQ RLQQLTANKG
     LSDNLINTTY FDRLGQIWIA TSSALNLMDT EGLMPKFLTA ADGLSGPDVW SFFEDNKAHL
     WIASRQGIDI YDPLSNTIRE VDHELGLNKA PNISYKILPM PTGEYLIVSP RFGLGIFSPE
     LQTIRIIGTE QGLNIPIPSS SLVDHRGHIW NGSFQNGTVE YMDSDTNTFK LFTNKNGLVG
     DIVWELMEDD KGQIWVATDK SINIINVADN TISQLMENGK ISERNGGAFL RDAKDRMWIA
     TRSGILIADQ NKGTLTSLNT ENGLVHKAVY TLYENEGKIY AGTENGFTVF TPKSEEELDD
     TFSYEVKSFG KGQGLKYTDF NAGAAIVYED KLWWGIETQA MTISNIPKEK STTSIAHIVG
     ITISDEPQTF YEYRTILQNY PKLDTLYTSK KDTFYISEKI PKESGGLREN NISWDSLDGY
     YNLPVNLKIP FEQNYLSFQF TGAQLTNIDK TRYRYILEGF DTEWSEITEI SNSKNYRNLA
     AGDYLFKVRS RTADGIWSEP AEMSFTILPH WTNTWWAWSL YVLAFIIVVG MIAQYRARLL
     KKENLILEEK VKHRTAQLNK SVEDLKATQS QLIQSEKMAS LGELTAGIAH EIQNPLNFVN
     NFSEVSNELI QEIQAERTKQ KENRDEKLVE EILVDIQENL EKINHHGKRA DAIVKGMLQH
     SRNSSGEKRL TDINALCDEY TRLSYHGLRA KDKSFNADIK TDFDENISKV EINQQDIGRV
     ILNLVNNAFY AVHEKKIKTN DKDYKPLVQI STQLDSGGII IQVKDNGNGI PDKVKEKIFQ
     PFFTTKPTGK GTGLGLSLSY DIIKAHNGQI NVETVEGENT KFTIFLPC
//
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