ID A9D9Y5_HOEPD Unreviewed; 694 AA.
AC A9D9Y5;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HPDFL43_08644 {ECO:0000313|EMBL:EDQ33004.1};
OS Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Hoeflea.
OX NCBI_TaxID=411684 {ECO:0000313|EMBL:EDQ33004.1, ECO:0000313|Proteomes:UP000004291};
RN [1] {ECO:0000313|EMBL:EDQ33004.1, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ33004.1,
RC ECO:0000313|Proteomes:UP000004291};
RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDQ33004.1, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ33004.1,
RC ECO:0000313|Proteomes:UP000004291};
RA Fiebig A.;
RL Submitted (JUN-2012) 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:EDQ33004.1}.
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DR EMBL; ABIA03000002; EDQ33004.1; -; Genomic_DNA.
DR RefSeq; WP_007197508.1; NZ_CM002917.1.
DR AlphaFoldDB; A9D9Y5; -.
DR STRING; 411684.HPDFL43_08644; -.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_396801_0_0_5; -.
DR OrthoDB; 9808408at2; -.
DR Proteomes; UP000004291; 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 CDD; cd00130; PAS; 2.
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; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF12860; PAS_7; 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; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000004291};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 336..406
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 409..460
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 478..693
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 694 AA; 77615 MW; 3B7292F81B6225C4 CRC64;
MLHFRKTLRW VLISVGATVL SLLIMSQFPN MAIPARYWIA AVLLPAVISY FVSRKLIQQT
EDLAVLNAAL MEANATLTSK LRAENLLNMA FSTISQGCSI YDENDCLVFC NDAYREIYSL
SATAILPGRC FGSMLRHGLE VGQYPEAGTT PEDQEAWLQK RMGRHRNPTG PFLQKIGPDS
WIQVEEYVTK ENYRIGLLTD VSALLQVKSE AEQLGHIIEA VAQEVYLIST ADGRIVNANK
AARTNLQYSL EELRGLTALD VNSGHSSLEM AETIAPIVAG ERKVVKINTE HRRKDGTTYK
CRVRLERLDD LSETVVVAFA EDVTERLEFE HAIERKQQEL ETLVRNLPDV ISRAEPDTTL
TYVNANYAEF TGVPVEDMIG CKFLEFSPTE NLDELTSHIE SLTPEQPIRL IEQPMYNSSG
EKRWYLWSNL MVFDEGEPVE LVSVGRDITE SRKAQERIAK QTRELALRND ALEQFGGIIS
HDLKAPLRQI RVFSEMIKED IELGKTDELA NWSSHVVNRA RSMEQMISSL FAYSRLAYQS
VHLEKFLLSE AISAAWENLS VSVADSRAQL VDRCDLMVTA DINLMTQLLQ NMFANSIKYT
EDGVAPQIRV SAETVGCATV IVVEDNGIGI ATVHAESIFG VFERLHPDET RYAGAGIGLA
LCRRVVESHG GTIALDSSYV DGARFVIRLP ALSL
//