ID   HSSS_STAAR              Reviewed;         457 AA.
AC   Q6GE72;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Heme sensor protein HssS;
DE            EC=2.7.13.3;
GN   Name=hssS; OrderedLocusNames=SAR2448;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Member of the two-component regulatory system HssS/HssR
CC       involved in intracellular heme homeostasis and tempering of
CC       staphylococcal virulence. HssS functions as a heme sensor histidine
CC       kinase which is autophosphorylated at a histidine residue and transfers
CC       its phosphate group to an aspartate residue of HssR. HssR/HssS
CC       activates the expression of hrtAB, an efflux pump, in response to
CC       extracellular heme, hemin, hemoglobin or blood (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 membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR   EMBL; BX571856; CAG41430.1; -; Genomic_DNA.
DR   RefSeq; WP_000477322.1; NC_002952.2.
DR   AlphaFoldDB; Q6GE72; -.
DR   SMR; Q6GE72; -.
DR   KEGG; sar:SAR2448; -.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OMA; IDNIAHE; -.
DR   OrthoDB; 1827824at2; -.
DR   Proteomes; UP000000596; Chromosome.
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; 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   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system; Virulence.
FT   CHAIN           1..457
FT                   /note="Heme sensor protein HssS"
FT                   /id="PRO_0000331341"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          186..238
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          246..456
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         249
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   457 AA;  52343 MW;  DD49A76C3BE13BE2 CRC64;
     MFKTLYARIA IYSITVILFS ALISFVLTNV YYHYNLKASN DAKIMKTLKE ARQYEQSAKP
     THIQQYFKHL GQMNYQIMTI DHKGHKTFYG EPFREDTLSQ NAINNVLNNK DYHGIKDKPF
     ALFVTGFFDN VTDNTVGINF KTNDGSIAVF MRPDIGETFS EFRTFLAVLL ILLLFISISL
     VIASTYSIIR PVKKLKLATE RLIDGDFETP IKQTRKDEIG TLQYHFNKMR ESLGQVDQMR
     QHFVQNVSHE IKTPLTHIHH LLSELQQTSD KTLRQQYIND IYTITTQLSG LTTELLLLSE
     LDNHQHLLFD DKIQVDQLIK DIIRHEQFAA DEKSLIILAD LESIDFLGNQ RLLHQALSNL
     LINAIKYTDV GGAIDIALQH SHNNIIFTIS NDGSPISPQA EARLFERFYK VSKHDNSNGL
     GLAITKSIIE LHHGTIQFTQ SNAYVTTFTI TLPNHSH