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Database: UniProt
Entry: F1W1X1_9BURK
LinkDB: F1W1X1_9BURK
Original site: F1W1X1_9BURK 
ID   F1W1X1_9BURK            Unreviewed;       840 AA.
AC   F1W1X1;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=IMCC9480_303 {ECO:0000313|EMBL:EGF31149.1};
OS   Oxalobacteraceae bacterium IMCC9480.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae.
OX   NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF31149.1, ECO:0000313|Proteomes:UP000004494};
RN   [1] {ECO:0000313|EMBL:EGF31149.1, ECO:0000313|Proteomes:UP000004494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF31149.1,
RC   ECO:0000313|Proteomes:UP000004494};
RX   PubMed=21572000; DOI=10.1128/JB.05088-11;
RA   Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT   "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT   betaproteobacterium isolated from the Arctic Ocean.";
RL   J. Bacteriol. 193:3421-3421(2011).
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:EGF31149.1}.
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DR   EMBL; AEPR01000505; EGF31149.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1W1X1; -.
DR   OrthoDB; 219325at2; -.
DR   Proteomes; UP000004494; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF55781; GAF 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; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGF31149.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004494};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..127
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          304..358
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          454..673
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          710..828
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         59
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         759
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   840 AA;  90865 MW;  31D292B44DFF2768 CRC64;
     MTRPWRILLV DDNPDDRADA KAALLKGSGR RYQFIEAALA QEALDYCAQQ PAPDCMLLDF
     DLPDADAFEL LARLPRDSHG ITLVPVVILT GSSRQSLSQE LLRAGAEDYV GKAWLGPESL
     TRGVENAVER HLMKRELWRE RARQQVIADI AQAATDGPGN AMAALFERVR VLVQADIFLS
     HVLDIGVPPM LRLTADAGID AATRLLYLLL DPVTSLCGSV IAHGKPVFRH HMREHDEEAT
     AVLKNIGVQA YASYPLQVDG RVIGTLSFGS RTRVAFDEDE CDFMGTVASQ VGAAWERLDL
     LRSKDNELRS MTDNSPDILT RFDRQLRHVF INAAITRVTG HPPAYFIGKS NREVGMPEAL
     CVRWERAMQH VFATGEAQQV SFDFQAVTGL RHFDCQLVAE QRGDGRILHI LGVTHDVTAR
     RQLDERREEL LEAERAARIE SERVALIKDE FLATLSHELR TPLSAIMGWA SLLKRAPPSP
     ELYRKGIDVI ARNATEQAAL IGDLLDMNRI LSGKLRMESE LVHLDAVAAA AIDTLAPAAL
     AKGIALELVL APAGPVRVLG DGARLQQVLW NLLANGVKFT ASGGVVTLAI DERDDLVVAT
     VTDNGNGIEA GFLPFLFDRF SQSDGSAARV HGGLGLGLSI VKNLLELHGG TVSASSGGAG
     RGACFTVLLP RAPDGPLPRM VPVAMPETLP EVLVTGPVSV DDSNALRGMA VLLVDDNPDV
     LELGRRLLTE HGALVTTAQS ADEALVQIRR QVPDILLSDI GMPGTDGYQL IELVRTGMGL
     GAAQLPAVAV TAYARAQDHA RALQAGYQAC IDKPIRPQLL IRTLLDLAVV KAAGTYPDGG
//
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