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Database: UniProt
Entry: A6GNX7_9BURK
LinkDB: A6GNX7_9BURK
Original site: A6GNX7_9BURK 
ID   A6GNX7_9BURK            Unreviewed;       756 AA.
AC   A6GNX7;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=LMED105_13343 {ECO:0000313|EMBL:EDM83963.1};
OS   Limnobacter sp. MED105.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Limnobacter.
OX   NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM83963.1, ECO:0000313|Proteomes:UP000010322};
RN   [1] {ECO:0000313|EMBL:EDM83963.1, ECO:0000313|Proteomes:UP000010322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED105 {ECO:0000313|EMBL:EDM83963.1,
RC   ECO:0000313|Proteomes:UP000010322};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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:EDM83963.1}.
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DR   EMBL; ABCT01000004; EDM83963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6GNX7; -.
DR   STRING; 391597.LMED105_13343; -.
DR   Proteomes; UP000010322; 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
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; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 3.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010322}.
FT   DOMAIN          20..84
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          271..341
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          388..460
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          464..516
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          529..752
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   756 AA;  85566 MW;  1C0EA92ABDA08DB8 CRC64;
     MHPEPFKIGD MKMDNNPLLL EENALQALSA LPQPIWIFDP ETLRIIWNNP ACEEWLEISA
     AELQSKTILD LRPPSDHQAL RAALIAFQNE TTFTSQWTLQ SKTSKSFKAR FHWQRCALNQ
     KIQVLATIND VTDTHETLAN LDRAKKLIDI AGTKAKLGGW RMSLGSDHVS WTPQTAAIHD
     APYEPAPSAE EAFSYYLPAY RQKIEKCYTE CITEGKPYDE ILQIKTRSNR IAWVRAIGEP
     ELDSLGNIIG AQGAFQDITE LIHEKNRNSD LEQRLFSTLE NMSDSFFMIS TRFDFVYLNP
     RAENLLKRRR EDLIGKNIWQ EFPEARNTPV YSLYQQAIDT GNAIKVKFFY PPLDTWFEVN
     GYPTSEGLGV YFRDVTNEEN QQQAAKLLHE RFVLVSKATN DVIWDWDLIK NGLWWNESMS
     RVFGYELLQL EPGPESWTTR IHPDDSQRVL ESIHQVIDGT GTHWSNEYRF AKSSGKYALV
     HDRGFVIRDE QGKAIRMLGS MLDLTETREL EEKLRESQKL EAMGQLTGGV AHDFNNLLTV
     IMGNAETLAY RLKDNPQLQS LAEMTSKAAE RGAELTSRLL SFARRQPLQP KTVDAGQLIQ
     DSLALFRRIL PETIEIEAPD TDGLWKIAVD PGQLEVALLN LVINGRDAIP QAGKLHISAL
     NTELDSIQTD AKETLPAGPY VLISVRDTGH GMTQETLNRA FEPFFTTKEV GKGSGLGLSM
     VFGFVKQSKG YIKIHSAPNS GTCVELYFPK FAPETP
//
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