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Database: UniProt
Entry: A3WFR8_9SPHN
LinkDB: A3WFR8_9SPHN
Original site: A3WFR8_9SPHN 
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
//
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