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Database: UniProt
Entry: A0A068QNP4_9GAMM
LinkDB: A0A068QNP4_9GAMM
Original site: A0A068QNP4_9GAMM 
ID   A0A068QNP4_9GAMM        Unreviewed;       565 AA.
AC   A0A068QNP4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=yehU {ECO:0000313|EMBL:CDG16191.1};
GN   ORFNames=XDD1_0488 {ECO:0000313|EMBL:CDG16191.1};
OS   Xenorhabdus doucetiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG16191.1, ECO:0000313|Proteomes:UP000032721};
RN   [1] {ECO:0000313|EMBL:CDG16191.1, ECO:0000313|Proteomes:UP000032721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA   Genoscope - CEA;
RL   Submitted (JUL-2013) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FO704550; CDG16191.1; -; Genomic_DNA.
DR   RefSeq; WP_045968336.1; NZ_VNHN01000005.1.
DR   AlphaFoldDB; A0A068QNP4; -.
DR   STRING; 351671.XDD1_0488; -.
DR   KEGG; xdo:XDD1_0488; -.
DR   HOGENOM; CLU_020473_3_3_6; -.
DR   OrthoDB; 2514702at2; -.
DR   Proteomes; UP000032721; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   PANTHER; PTHR34220:SF10; SENSOR HISTIDINE KINASE BTSS; 1.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:CDG16191.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:CDG16191.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        141..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          218..365
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   565 AA;  62476 MW;  7955D6BAFA7FD6DB CRC64;
     MYEFNLVLLL LQQMCVYLVI AWLLSKTPLF IPLLQVTVRL PHKLMCYVIF SIFCIMGTYF
     GLNVNDSIAN TRAIGAVLGG FLGGPTVGAM VGFTGGLHRY SLGGMTAFSC MVSTIVEGVL
     GGLVHIYLMK KGQLNKLLNP WTAAVVTFFA ECTQMGIILL LANPFGEALS LVKDIAAPMI
     IANSIGAAMF IRILLDRRAI FKKYTSAFSA QALKIAVCTE GILRKGFNED NSMRVAKVIY
     QELEIGAVAI TDREKLLAFI GIGSDHHLPG TPIAAKQSRR AIENNEVVYA DGNETPYCCS
     LSPTCKLGSA LVIPLRGENQ QVIGTIKLYE AKNRLFSSIN RTLGEGIASL LSAQILAGQY
     ERNKQSLLQS EIKLLHAQVN PHFLFNALNT LQAVIRRDSQ QAGQLVQYLS TFFRKNLKRP
     EDIATLDNEI EHVNAYLQIE KARFREHLQI AIEIPESLRN ARLPAFSLQP MVENAIKHGT
     SQLLETGRIT IRAHQEANLL LVEIEDNAGL YCPQKMGDGL GMSLVDKRLR LRYGTQYGVR
     VDCQPEAFTR VILCLPLEKE TKKAA
//
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