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
//