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Database: UniProt
Entry: Q3YZ84_SHISS
LinkDB: Q3YZ84_SHISS
Original site: Q3YZ84_SHISS 
ID   Q3YZ84_SHISS            Unreviewed;       566 AA.
AC   Q3YZ84;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 125.
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:AAZ89178.1};
GN   OrderedLocusNames=SSON_2549 {ECO:0000313|EMBL:AAZ89178.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ89178.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ89178.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ89178.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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}.
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DR   EMBL; CP000038; AAZ89178.1; -; Genomic_DNA.
DR   RefSeq; WP_005143133.1; NC_007384.1.
DR   AlphaFoldDB; Q3YZ84; -.
DR   KEGG; ssn:SSON_2549; -.
DR   HOGENOM; CLU_000445_20_10_6; -.
DR   OMA; IKHSQGT; -.
DR   Proteomes; UP000002529; Chromosome.
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   CDD; cd06225; HAMP; 1.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   CDD; cd22899; NarQ_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 1.20.120.960; Histidine kinase NarX, sensor domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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   PANTHER; PTHR24421:SF10; NITRATE/NITRITE SENSOR PROTEIN NARQ; 1.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
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; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 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|PIRNR:PIRNR003167};
KW   Cell membrane {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|PIRNR:PIRNR003167};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002529};
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        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          174..227
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          364..559
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   566 AA;  63617 MW;  C962C3C878A081A5 CRC64;
     MIVKRPVSAS LARAFFYIVL LSILSTGIAL LTLASSLRDA EAINIAGSLR MQSYRLGYDL
     QSGSPQLNAH RQLFQQALHS SVLTNLNVWY VPEAVKTRYA HLNANWLEMN NRLSKGDLPW
     YQANINNYVN QIDLFVLALQ HYAERKMLLV VAISLAGGIG IFTLVFFTLR RIRHQVVAPL
     NQLVTASQRI EHGQFDSPPL DTSLPNELGL LAKTFNQMSS ELHKLYLSLE ASVEEKTRDL
     HEAKRRLEVL YQCSQALNTS QIDVHCFRHI LQIVRDNEAA EYLELNVGEN WRISEGQPNP
     ELPMQILPVT MQETVYGELH WQNSHVSSSE PLLNSVSSML GRGLYFNQAQ KHFQQLLLME
     ERATIARELH DSLAQVLSYL RIQLTLLKRS IPEDNATAQS IMADFSQALN DAYRQLRELL
     TTFRLTLQQA DLPSALREML DTLQNQTSAK LTLDCRLPTL ALDAQMQVHL LQIIREAVLN
     AMKHANASEI AVSCVTAPDG NHTVYIRDNG IGIGEPKEPE GHYGLNIMRE RAERLGGTLT
     FSQPSGGGTL VSISFRSAEG EESQLM
//
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