ID   IRLS_BURP2              Reviewed;         464 AA.
AC   I1WSZ3; O31396; Q63LH6;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Sensor protein IrlS;
DE            EC=2.7.13.3;
GN   Name=irlS; OrderedLocusNames=BP1026B_II1138;
OS   Burkholderia pseudomallei (strain 1026b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=884204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1026b;
RX   PubMed=9393784; DOI=10.1128/iai.65.12.4972-4977.1997;
RA   Jones A.L., Deshazer D., Woods D.E.;
RT   "Identification and characterization of a two-component regulatory system
RT   involved in invasion of eukaryotic cells and heavy-metal resistance in
RT   Burkholderia pseudomallei.";
RL   Infect. Immun. 65:4972-4977(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1026b;
RX   PubMed=22615773; DOI=10.1371/journal.pone.0036507;
RA   Hayden H.S., Lim R., Brittnacher M.J., Sims E.H., Ramage E.R., Fong C.,
RA   Wu Z., Crist E., Chang J., Zhou Y., Radey M., Rohmer L., Haugen E.,
RA   Gillett W., Wuthiekanun V., Peacock S.J., Kaul R., Miller S.I., Manoil C.,
RA   Jacobs M.A.;
RT   "Evolution of Burkholderia pseudomallei in recurrent melioidosis.";
RL   PLoS ONE 7:E36507-E36507(2012).
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.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF005358; AAB92483.1; -; Genomic_DNA.
DR   EMBL; CP002834; AFI69387.1; -; Genomic_DNA.
DR   RefSeq; WP_004184766.1; NZ_CP004380.1.
DR   AlphaFoldDB; I1WSZ3; -.
DR   SMR; I1WSZ3; -.
DR   EnsemblBacteria; AFI69387; AFI69387; BP1026B_II1138.
DR   GeneID; 56597412; -.
DR   KEGG; bpz:BP1026B_II1138; -.
DR   PATRIC; fig|884204.3.peg.5415; -.
DR   BRENDA; 2.7.13.3; 1031.
DR   Proteomes; UP000010087; 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; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system; Zinc.
FT   CHAIN           1..464
FT                   /note="Sensor protein IrlS"
FT                   /id="PRO_0000429789"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
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;  50653 MW;  C4FE275489AEDCBD 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 EPMAEDAEVS IVVRGKAEVR ADALLYHRAL
     SNLISNALNH APRGSTITIE CAQAADAATI SVSDTGRGIE APHRERIFER FYRVDPARHN
     SASGTGLGLA IVRSIMENHG GTCGVDSEPH VRTTFWLKFP AHAA