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Database: UniProt
Entry: A0A1W6Z3S8_9BORD
LinkDB: A0A1W6Z3S8_9BORD
Original site: A0A1W6Z3S8_9BORD 
ID   A0A1W6Z3S8_9BORD        Unreviewed;       770 AA.
AC   A0A1W6Z3S8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CAL13_17985 {ECO:0000313|EMBL:ARP87891.1};
OS   Bordetella genomosp. 9.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416803 {ECO:0000313|EMBL:ARP87891.1, ECO:0000313|Proteomes:UP000194139};
RN   [1] {ECO:0000313|EMBL:ARP87891.1, ECO:0000313|Proteomes:UP000194139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17164 {ECO:0000313|EMBL:ARP87891.1,
RC   ECO:0000313|Proteomes:UP000194139};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) 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; CP021109; ARP87891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6Z3S8; -.
DR   Proteomes; UP000194139; Chromosome.
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; 2.60.40.2380; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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   PANTHER; PTHR43711:SF29; SENSOR HISTIDINE KINASE HIK2; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF07696; 7TMR-DISMED2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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   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:UP000194139};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..770
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013297960"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        346..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        387..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          466..681
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          412..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  82596 MW;  44810C253C45F003 CRC64;
     MQVNLKRFAI LAITAITLCA GSASAPSKAS PVVDYPAVDS AAPISLRPYT QVYEDRDGRL
     ALADILAIEK SDPHRFRPLK EMRRLGAYSG SAWWLRTEIV NAAKAPHALI LVGGPPNLEQ
     VDFYLQQDGQ WRHFPAGTMI PALQKDGATG YPAAQFTAAP GEAVAVWIRI ESASPIRLEP
     ALYTPGSFVA ARASDNILGG VLTSSIAALG ICAFILFAAS HRRAFLWFGG ICVTIALSEA
     ASRAYIQPVF WSMASGWTYR LETVIHAIGA ALTAMFVYAM GQRAGLPAGH RKVYGVIAAL
     LVICIVPTHF LPVAVLSMAT LALTVVMGIC LMTSALGTAR LSRNGAILLA AAAVLLLAHA
     AGMSLHLPGA SPWLIPSALP QAGTPPVALF SMLACAVALT LWATHRRKSQ RVAPGNKQLA
     AKETGSLERD AAPPHAQVPP ATPAAVAPRD EAGHLATPQQ TLVLGYVGHD LRAPLATISG
     YARLLRQTAR PEQESYLDMI ERSINYQFSL IDEILAYAEY DLQPFDISAG DVQLPALLEE
     LARFGVSLCN HQGNAFRYIP ATQLPAVVRL DAKRTRQAVL NLLGNAAKFT RDGTVCFEAG
     VNQRDDGAEL MLQVTNDGTP IPVEHQAEIF SAFRQLRHRD AGSGLGLFIA DRIVHGMGGS
     LRFDSSPKLG NRFAITLPIA VADATPIVTR PIHHVAARDG GTQGIAAPPL AARLALAKLA
     REGELSEIQQ WTAETRQHHP QYEAFYRAVD QCVDNFDMEC LQRLALLGIT
//
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