ID A3WFR8_9SPHN Unreviewed; 408 AA.
AC A3WFR8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NAP1_13388 {ECO:0000313|EMBL:EAQ28595.1};
OS Erythrobacter sp. NAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ28595.1, ECO:0000313|Proteomes:UP000002995};
RN [1] {ECO:0000313|EMBL:EAQ28595.1, ECO:0000313|Proteomes:UP000002995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAP1 {ECO:0000313|EMBL:EAQ28595.1,
RC ECO:0000313|Proteomes:UP000002995};
RX PubMed=21952547; DOI=10.1128/JB.05845-11;
RA Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S.,
RA Falkowski P.G.;
RT "Genome Sequence of the Marine Photoheterotrophic Bacterium Erythrobacter
RT sp. Strain NAP1.";
RL J. Bacteriol. 193:5881-5882(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:EAQ28595.1}.
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DR EMBL; AAMW01000002; EAQ28595.1; -; Genomic_DNA.
DR AlphaFoldDB; A3WFR8; -.
DR STRING; 237727.NAP1_13388; -.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_020473_1_1_5; -.
DR Proteomes; UP000002995; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EAQ28595.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002995};
KW Transferase {ECO:0000313|EMBL:EAQ28595.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..366
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 367..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 408 AA; 44715 MW; 95F468EB260330F6 CRC64;
MRIQPAPFFA SKNRAFWNLQ LAGWGGYFLL RTVVAVANDQ PLNLLAVLVV TTVTGFSISL
ILSVIYRQLI DRQPIVTWGG SAVALMGAVI VYASIDAWLQ GLYYGAARET TFAQRFIGLS
FIPLTLLGAW SALYYAINFF LTVEKQADRL ERLEAQTTAA QLAMLRYQLN PHFLFNTLNS
ISTLVLLKQT EPANAMLTRL SGFLRHTLIT EPGSQVTLAQ EVETLKLYLD IERMRFEERL
RTHFEIDDAA MDACLPAMLL QPLIENAIKY AVSPQEEGAR ISLTARVIGE RLRIAVEDTG
PGIEGPVQLS MLEHLPEGAG KPVSTGVGLA NIRNRLMQGY GEDHVFETTS QPGGGFTVLI
EIPFEPVEKS QSAPSAASKG RPAKSASPAN ETPDNVVALN PQRAIGNT
//