ID   HSSS_STAA1              Reviewed;         457 AA.
AC   A7X5Y6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Heme sensor protein HssS;
DE            EC=2.7.13.3;
GN   Name=hssS; OrderedLocusNames=SAHV_2346;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF79229.1; -; Genomic_DNA.
DR   RefSeq; WP_000477338.1; NC_009782.1.
DR   AlphaFoldDB; A7X5Y6; -.
DR   SMR; A7X5Y6; -.
DR   KEGG; saw:SAHV_2346; -.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OMA; IDNIAHE; -.
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_0000331343"
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;  52386 MW;  49A0FB54D4CD1503 CRC64;
     MFKTLYARIA IYSITVILFS ALISFVLTNV YYHYNLKASN DAKIMKTLKE ARQYEQSAKP
     THIQQYFKHL GQMNYQIMTV DQKGHKTFYG EPFREDTLSQ NAINNVLNNK DYHGIKDKPF
     ALFVTGFFDN VTDNTVGINF KTKDGSIAVF MRPDIGETFS EFRTFLAVLL MLLLFISISL
     VIASTYSIIR PVKKLKLATE RLIDGDFETP IKQTRKDEIG TLQYHFNKMR ESLGQVDQMR
     QHFVQNVSHE IKTPLTHIHH LLSELQQTSD KTLRQQYIND IYTITTQLSG LTTELLLLSE
     LDNHQHLLFD DKIQVDQLIK DIIRHEQFAA DEKSLIILAD LESINFLGNQ RLLHQALSNL
     LINAIKYTDV GGAIDIALQH SHNNIIFTIS NDGSPISPQA EARLFERFYK VSKHDNSNGL
     GLAITKSIIE LHHGTIQFTQ SNEYVTTFTI TLPNNSH