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Database: UniProt
Entry: A0A117SEP2_9FLAO
LinkDB: A0A117SEP2_9FLAO
Original site: A0A117SEP2_9FLAO 
ID   A0A117SEP2_9FLAO        Unreviewed;       684 AA.
AC   A0A117SEP2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=APF83_13900 {ECO:0000313|EMBL:KUO67205.1};
OS   Lutibacter sp. BRH_c52.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=1734397 {ECO:0000313|EMBL:KUO67205.1, ECO:0000313|Proteomes:UP000054346};
RN   [1] {ECO:0000313|EMBL:KUO67205.1, ECO:0000313|Proteomes:UP000054346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c52 {ECO:0000313|EMBL:KUO67205.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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:KUO67205.1}.
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DR   EMBL; LOEY01000045; KUO67205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117SEP2; -.
DR   Proteomes; UP000054346; 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; 1.25.40.10; Tetratricopeptide repeat domain; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43711:SF32; DRUG SENSORY PROTEIN A; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13424; TPR_12; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00028; TPR; 7.
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; SSF48452; TPR-like; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50005; TPR; 4.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        399..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          81..114
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          121..154
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          161..194
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          241..274
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          465..683
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   684 AA;  78062 MW;  1A438AD94BF689C9 CRC64;
     MKNRLIILFY LGFSSLIIGQ EAADINKLKK ELQQELVDTA KVTLHLKIAN LYLKTKPDSS
     LVNLTKALEL AKKSAYQPKI AQVYNRIGRY YEKIVDYKDA IKNYNDAFLI FEKLGDKKKM
     AEIYNSLGTN YSELYAEDRA IEYYLKSLAF HKEVQDQKGI ASNYTNIGNL YYNEENYDLA
     EKYFRDALLI YEKLDDKYGI SSSYTNIANA LADNGRVEEG LNYYKKSIAI EDKLGDQYGI
     AINYNNIGDC YINLKQYIQA MEYLDKAMKI ADSLGEKDLQ SIVLLNIADV ENKQKRFQRA
     IYAARESYAI ADLIGNLDYK TENLLQASIA YEGLGDNALA LKRLKEYTTI KDSLLKMDRL
     KKIKLFNTLN ELEKSQYTIE DLSKTSEEAQ LNYEKEKKYT HFLIIAIVVF AFLLILLIQQ
     NASKKKAFNL LEYKNYQVHK MKDEIDGQSN KLKQLNSTKD KFFSIIAHDL KNPFNSIAGF
     TELMIENNEI YDKEKRLKFL KIIKGSSAKV SSLLDNLLIW ASSQSGNLKF NPKNINLALQ
     VTGVISFLEI QAINKDIAIL NRVEKNVYVK ADENMLDTIL RNLISNAIKF TQPKGEIHIY
     SVLKKDFVEI TVKDNGVGMS ADEIAAIFSV NEINSSLGTF NEQGSGLGLI LCSDFVESHG
     GKIWVESVVN QGSEFKFTLP IWKD
//
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