ID   A0A7Y4EUZ7_VIBAN        Unreviewed;       574 AA.
AC   A0A7Y4EUZ7;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE            EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
GN   Name=narQ {ECO:0000313|EMBL:NOI06732.1};
GN   ORFNames=F0263_17090 {ECO:0000313|EMBL:NOI06732.1};
OS   Vibrio anguillarum (Listonella anguillarum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=55601 {ECO:0000313|EMBL:NOI06732.1, ECO:0000313|Proteomes:UP000563949};
RN   [1] {ECO:0000313|EMBL:NOI06732.1, ECO:0000313|Proteomes:UP000563949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=00-84-1 {ECO:0000313|EMBL:NOI06732.1,
RC   ECO:0000313|Proteomes:UP000563949};
RA   Kehlet-Delgado H., Mueller R.S.;
RT   "Draft genome sequencing and comparative genomics of hatchery-associated
RT   Vibrios.";
RL   Submitted (SEP-2019) 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         ECO:0000256|PIRNR:PIRNR003167};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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:NOI06732.1}.
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DR   EMBL; VTYO01000033; NOI06732.1; -; Genomic_DNA.
DR   Proteomes; UP000563949; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.960; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR029095; NarX-like_N.
DR   InterPro; IPR042295; NarX-like_N_sf.
DR   InterPro; IPR016380; Sig_transdc_His_kin_NarX/NarQ.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF13675; PilJ; 1.
DR   PIRSF; PIRSF003167; STHK_NarX/NarQ; 2.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR003167};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW   ECO:0000256|PIRNR:PIRNR003167};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR003167};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR003167};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003167};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR003167};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003167};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW   ECO:0000256|PIRNR:PIRNR003167}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          176..228
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          368..567
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   574 AA;  64386 MW;  84DB37489FBF4B06 CRC64;
     MRKRSKQSVT STIAKAMVSI LLLSVAITGY AIFTLASSLN DAEAVNVAGS MRMQSYRLAH
     DIQSNSVDYS SHIYLFERSL YSPSMKALQR WPVPNDITKD YYQLIIRWHE LKSLLNSENK
     DRYLDEVAKF VSQIDRFVFK LQHFSEQKLI QLAWFGGMGL GGVLCISLFV VHFIRKEVVG
     PLRSLVTASE QIQNRSFDVS LNVTSHNEMG ILTRTFNKMA TDLGKLYLGL EQAVNEKTHK
     LQNANQALQV LYDCSQELTA SRISQDNFQA ILQHLVTIEG VTFAQLEIGD DAGKSTRLSE
     GESNGFSLSP LLLSLDGMQL GYLYLQYSLP CPNSALIDNF VQILSRAIYY NQAQKQAEQL
     ILMEERATIA RELHDSLAQS LSYLKIQVSL LKRVIGRAET PHAAEKKEQI ILDIDQGLSG
     AYTQLRELLT TFRLTIKEGN FGQALKGMLE ELGEQTTAEI VLNNNLSSID LDAHQQVHLL
     QLIREATINA IKHAQANAIQ VNCDELDDQV MVTVKDDGVG FDQQRARLNH YGLSIMQERA
     ARLHGAVSVT SAPNAGCEVI LKYKRSKDTN FDEM
//