ID   IRLS_BURPS              Reviewed;         464 AA.
AC   P0DMK6; O31396; Q63LH6;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Sensor protein IrlS;
DE            EC=2.7.13.3;
GN   Name=irlS; OrderedLocusNames=BPSS1039;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- FUNCTION: Member of the two-component regulatory system IrlR/IrlS. May
CC       be involved in invasion of eukaryotic cells and heavy-metal resistance.
CC       Probably activates IrlR by phosphorylation (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
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DR   EMBL; BX571966; CAH38500.1; -; Genomic_DNA.
DR   RefSeq; WP_009971776.1; NZ_CP009537.1.
DR   RefSeq; YP_111045.1; NC_006351.1.
DR   AlphaFoldDB; P0DMK6; -.
DR   SMR; P0DMK6; -.
DR   STRING; 272560.BPSS1039; -.
DR   EnsemblBacteria; CAH38500; CAH38500; BPSS1039.
DR   KEGG; bps:BPSS1039; -.
DR   PATRIC; fig|272560.51.peg.4227; -.
DR   eggNOG; COG0642; Bacteria.
DR   OMA; DLVMGHD; -.
DR   Proteomes; UP000000605; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR006290; CztS_silS_copS.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR01386; cztS_silS_copS; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cadmium; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix; Two-component regulatory system; Zinc.
FT   CHAIN           1..464
FT                   /note="Sensor protein IrlS"
FT                   /id="PRO_0000074770"
FT   TOPO_DOM        1..13
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..166
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..464
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          188..241
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          249..463
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         252
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   464 AA;  50708 MW;  C54E26E488AEDD0D CRC64;
     MIRRLLPRTL RARLTALIIL STAATLALSG VALYSALHNR LVGMSSYEMS ATLAAMRTHL
     ANVANVDDIP RKSDLWIDQL HGHQNLDLAI YDTDGRLRFA TRGFVAPRPA LGAPQTRVPA
     SAAPAGATFS YLADDAPLRG GNPRTARIVV QYDGKNDHAL LRAYAYTVVV IEVLAVVLTA
     ALAYGIAMLG LSPLRRLVAR AEQMSSSRLA QPLPELDTSG ELKEMEHAFN AMLKRLDESF
     VRLSQFSSNL AHDMRTPLTN LLAEAQVALS KPRTADEYRD VIESSIDEYQ RLSRMIEDML
     FLARSDNAQS HLAIRTLDAA AQAERVAGYY EPMAEDADVR IVVRGKAEVR ADALLYHRAL
     SNLISNALNH APRGSTITIE CAQAADAATI SVSDTGRGIE APHRERIFER FYRVDPARHN
     SASGTGLGLA IVRSIMENHG GTCGVDSEPH VRTTFWLKFP AHAA