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Database: UniProt
Entry: A0A0S1Y5K5_9BORD
LinkDB: A0A0S1Y5K5_9BORD
Original site: A0A0S1Y5K5_9BORD 
ID   A0A0S1Y5K5_9BORD        Unreviewed;       774 AA.
AC   A0A0S1Y5K5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASB57_21390 {ECO:0000313|EMBL:ALM85190.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM85190.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM85190.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM85190.1,
RC   ECO:0000313|Proteomes:UP000064621};
RA   Hou L.;
RT   "Draft genome of Bordetella sp. N.";
RL   Submitted (NOV-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};
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DR   EMBL; CP013111; ALM85190.1; -; Genomic_DNA.
DR   RefSeq; WP_057654041.1; NZ_CP013111.1.
DR   AlphaFoldDB; A0A0S1Y5K5; -.
DR   STRING; 1746199.ASB57_21390; -.
DR   OrthoDB; 9815750at2; -.
DR   Proteomes; UP000064621; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS 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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR017232; NtrY.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
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; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PIRSF; PIRSF037532; STHK_NtrY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ALM85190.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064621};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          316..368
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          524..755
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   774 AA;  84678 MW;  4256710DFDB2E2BA CRC64;
     MRKLLRFALV AGALAGVLLL GLLAWSTGNA SRFARYYDAL LILNGVVALA LFAWVLALTV
     KLVRQIRRRQ FGARLTARFA LAFTLIGVVP GALIYTLSVQ FMSRSIESWF NVRVDSALEA
     GLNLGRAALD SLLADLDARA RSMTAELNRA SDSNIALTLT RLREANGVQE AMVFTGTGRM
     VAFSTNQYGQ LLPALPPSTV LNQLRLSRGY SAAEADDPVK GDGGGALHLR VVIPLLPNER
     FDGLLGASAE PRWLQLVQPV PDQIAHNANL VQQGFRDYQE LALARLGLRK LYGITLTLAL
     LVSVFTAIAV ALSLSKRLVR PLLRLAAGTQ AVGIGDFRPL PEPPERDEVG QLTRSFNAMT
     RQLDEARRMV ESNRQQLERS NVYLESVLSN LSSGVLVFDE AFRVTTVNQG AQTILQTDLR
     SVIGRPLETI DGMLPFTQVV RQAFTAHAAV GSERQHWQQQ FEIQLAQADA DAPAGPHAQS
     LTLLARGTHL RVDGRGNGYL VVFDDITELM SANRTVAWGE VARRLAHEIK NPLTPIQLSA
     ERLAMKLADR LQPADRQMLE RSTNTIVNQV SSLKHMVDDF REFARTPPAV MQRIDFNALV
     ADVLSLYGWD PVEGLVRDHS NSLNLEVELA PGLPAIEGDP TQLRQVIHNL LANARDAIAG
     QAEGRVRVST QLTQTPRNEG EEHRALRFTV SDTGPGFSQQ VMQRAFEPYV TTKSHGTGLG
     LAIVRKIVEE HGGRIDLANR REGGARISIL LTRLAGAVDT LDASAQQQDN AATQ
//
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