ID A0A1G6BGK1_9FLAO Unreviewed; 2311 AA.
AC A0A1G6BGK1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN03097699_0045 {ECO:0000313|EMBL:SDB19724.1};
OS Flavobacteriaceae bacterium MAR_2010_188.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250295 {ECO:0000313|EMBL:SDB19724.1, ECO:0000313|Proteomes:UP000199442};
RN [1] {ECO:0000313|EMBL:SDB19724.1, ECO:0000313|Proteomes:UP000199442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2010_188 {ECO:0000313|EMBL:SDB19724.1,
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; SDB19724.1; -; Genomic_DNA.
DR STRING; 1250295.SAMN03097699_0045; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000199442; Chromosome i.
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; 3.10.450.50; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR037401; SnoaL-like.
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; PF13474; SnoaL_3; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SDB19724.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199442};
KW Transferase {ECO:0000313|EMBL:SDB19724.1}.
FT DOMAIN 2073..2311
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 2034..2064
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2311 AA; 267260 MW; 3AECDA8CA283D69A CRC64;
MNLEKETHAE VKEVYDTWLH SYLVGDIAIY DSYLDDDYHF IGSTANEEFL NRKNTTNFLE
STADQLAGKT KLENNEYTFE EFNGLIFITH LFDAWFLAEE WKYYGRFRFT SALRKNTEGW
RFIYQHFSTP DTKAQEGETI GYEKISEENI QLRGAIKRRT IELEERNRQL EIEAALERVR
TKAMSMDTSN DLDNTVALVF KELENLGLKT IRCGIGIFDD RSNKVNVWSA SKPKDKNIAN
LSGDEYLEGH PLLDSIYENW TKQQDFEYTL EGQDLINYYK KVSKTNLPVS GPDKLRLDSK
QYYYVAMFPA GGLFAFKETR FNAEVRQLMK RFSEVFHLAF IRHQDLMKAE SQTKEAQVEL
ALERVRAKTM AMQHSDKLQF AAMELFHQLE ALKIPLFGCG FNIWDEDGET ATSWMAGKER
LQPSFKTSSK EDIFREIYES SKKGESLFVK EQKGKALERH YKYMASLPVF KEVIDRMEQT
GVPLPSFQIM HCAFFTKGYL MVITHKNVSD AYNIFIRFAK VFDQTYTRFL DLKKAEAQAR
EAQIEAALER VRSRSLAMHK SDELGDLSFE LVKQVQALGV ATWFCAFNIY DDEKGSLEWG
SNGEGVFPNY RTPREGIFLR YYKVGQSGET LLVNEIGEDE CPAHYEYLCT LPGVGEQLQQ
MKDAGIPFPA SQIDHVAFFK YGYIIFITYE PVPEAHNIFK RFAKVFEQSY TRFLDLKKAE
SQAREAEIQL ALERVRARTM AMQYSEELVE TSELLFQQIK DLGIEPWSCG FSLWYDDDSY
FLGYNPGPDG KMGPPLKIPL TEDIFFKTIR KAKREGIEFL VFESKGKSLV KTYEYMDGLP
VVGETMRAIV ASGFDLPTYQ VNHCGFFSHG HLMFITQEHY PEAHDIFIRF TREFEQTYTR
FLDLQKAEAQ AKEAQIEASL ERVRSKTMAM HSSQDVGNTM VLLFEELESL GIKANRNGII
ILDEEEHGEI WTAKPNINYE IELMAWQLDM SLHGLTKQVY KAWKNKNSGT IYPLIGDDLK
AYYKTLNKYT DIPVKFNLDT FPEREWCYTF NFNEGFIYLF TDEEILQEHE QIPVRFASVF
GQTYRRYQDL KKAEAQAREA KIEAALERVR SRSMAMHQSD EIGEVAKVLF EQLTGLGGEL
WGTGFAFCKK NSTEDEFWFV NERGIMPYLK IPNNVDSVHK KMHKGWQDQL EIFSIAKEGK
ELEAHYNYML SVPDVQPIFQ EMLDSGITFP KWQKWHAAYY KYGYLLVITT KPYEDEEIFI
RFAKVFEQTY TRFLDLKKAE SQTREAQINL AVERVRAKAL AMHKSEEIMD VVAKLKEEVM
ALDIPDVIAA TIFLKEGEDR VRMWDLSSLE KDNDGYQIPF DITFKLKKRD PNLYVKRVWE
NPENYFLEVQ EEKDFKRICQ WLRENNKTEV ADEVEEFIET TQLKKLHHAV KKLNNGKLVI
DLLNTPSDEM ETILTKMGAA FDLAYKRFED LQKAESQARE AQIEAALEKV RSQSLAMQKP
EELVDVVKVI VAKLKELDVI LDANGVILCT YFKDSKNVLH WIVSPDFSFA GSYLLPYFNH
PIFNKAWRSK ENGDAYFSEA FTVEEKNTFF EYAFEHSDYK DFPEDFKQWI FNNDKHTLSF
AWQKNSAILI PSHTGIVPNE GEKEILKRFS NVFEQAYIRF MDLQKAEAQA REAQIEAALE
RVRSKAMAMR SSEDISEATT VLFREIEKLE IETMRCGILI IHENKVMDVW TSSSNDNDEV
IRVTGQIDMT IHPLLINVYE QWQVGKSYSE FELSGKNGED YYQALRKEAN YELPTSFAVK
DLHYCFSFNF KEGAFFAFTR HRIPEKAMAV FERFARVFGL TYQRYQELIE SEKREKEAVK
QSSLDRVRAE IASMRNTEDL ERITPLIWGE LLTLGVPFFR CGLMIINDNE EKVRFYLSTP
EGRPLAALNL DYQSNDITSN GIKHWKKQQT YIAHWNKEEF LAFTKTLIEQ QQIDNPTTYL
GGEEAPESLT LQFVPFPQGM LYVGSAEDLS SSELDLVKNL ANAFSVAYAR YEDFNKLEIS
KLKIEQTLKE LKSTQNQLIQ SEKMASLGEL TAGIAHEIQN PLNFVNNFSE LSNELIDEMN
AEIEKGDIEE AKFIAKDIKA NLEKINHHGK RADSIVKGML QHSRSNSGTK EPTNINKLAD
EYLRLAYHGL RAKDKSFNVN LVTDFDESIG KVSVIPQDLG RVILNLITNA FYAVDKKKKS
VIENHEPTVK ISTKKLQNGI AITVKDNGSG MPAEVVDKIF QPFFTTKPTG EGTGLGLSLC
YDIIKAHNGE INVETQEGQG TTFILNLPYQ E
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