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Database: UniProt
Entry: A0A059KGN8_9BURK
LinkDB: A0A059KGN8_9BURK
Original site: A0A059KGN8_9BURK 
ID   A0A059KGN8_9BURK        Unreviewed;       781 AA.
AC   A0A059KGN8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=X805_39040 {ECO:0000313|EMBL:KDB50505.1};
OS   Sphaerotilus natans subsp. natans DSM 6575.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB50505.1, ECO:0000313|Proteomes:UP000026714};
RN   [1] {ECO:0000313|EMBL:KDB50505.1, ECO:0000313|Proteomes:UP000026714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB50505.1,
RC   ECO:0000313|Proteomes:UP000026714};
RX   PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA   Park S., Kim D.H., Lee J.H., Hur H.G.;
RT   "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT   formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL   FEMS Microbiol. Ecol. 90:68-77(2014).
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:KDB50505.1}.
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DR   EMBL; AZRA01000133; KDB50505.1; -; Genomic_DNA.
DR   RefSeq; WP_037485684.1; NZ_AZRA01000133.1.
DR   AlphaFoldDB; A0A059KGN8; -.
DR   STRING; 34103.SAMN05421778_11646; -.
DR   PATRIC; fig|1286631.3.peg.3795; -.
DR   eggNOG; COG5000; Bacteria.
DR   Proteomes; UP000026714; 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; 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
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; PF13188; PAS_8; 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   SMART; SM00091; PAS; 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.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KDB50505.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          326..378
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          390..430
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          526..756
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          752..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   781 AA;  83877 MW;  59A0F676A4D766DE CRC64;
     MSRSSLRWTV LIALLAIGGT VLVLAFLLSI ATNNRVLYER HYEWLLWVNI GVAASLGLVI
     VAALAQLVRR MRHGKFGSRL LVKLAAIFAF VGVVPGMLIY GVSYQFVSRS IESWFDVEVE
     GALESGLNLG RTTLQLLVND VAAKTRQAAE TSAESGADPG SRVQLLMLER LREQLAAQSV
     AVLSGSGQVL ASAGGAVGAA MLPDRPSPSL LRQARSQRVF AQLEGLDADT PIDGAITSGG
     PVRVRAIAWM PSTSLSLDSA DRYLQITQTV PQELVGNALR VQQAYSEYQE RALGREGLKR
     MYIGTLTLTL ILGIFSALLM AAGLGHQIGR PLVMLAEGVR QVARGDLRPT AVFASRDELG
     GLTRSFADMT QQLADARGLV QRSLAEAESA KAHLQTILDN LSSGVIVFEA DGRIDTVNPG
     AARILSLDPS AWTRHPIDRL PGLETFSAAV LARFEAHLRD LEDTGDEPAG DAHWQESLEL
     GSTEAPQTLL VRGALLPEGA RLLVFDDISD VVVAQRSVAW AEVARRLAHE IKNPLTPIQL
     SAERLQHKLE AKLTGTDQQM LVRSVGTIVT QVQAMKTLVN EFRDYARLPS ARLEPLDLNA
     LVVEVLGLYA AQQESGRLRA ELAPELPLLA GDASQLRQVI HNLVQNALDA VADLPDGLAI
     VSTECTRPDD GQTRAIRLKV MDNGPGFSEK VLKRAFEPYV TTKARGTGLG LAVVKKIVEE
     HGARIRLGNL ADEAQDPAAG PARTGAQVSI SFSRWARGGG TPAGNEPGRH RIPPSPDVSA
     S
//
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