ID   HSSS_STAHJ              Reviewed;         456 AA.
AC   Q4L8M0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Heme sensor protein HssS;
DE            EC=2.7.13.3;
GN   Name=hssS; OrderedLocusNames=SH0696;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04005.1; -; Genomic_DNA.
DR   RefSeq; WP_011275021.1; NC_007168.1.
DR   AlphaFoldDB; Q4L8M0; -.
DR   SMR; Q4L8M0; -.
DR   STRING; 279808.SH0696; -.
DR   PRIDE; Q4L8M0; -.
DR   EnsemblBacteria; BAE04005; BAE04005; SH0696.
DR   GeneID; 58063115; -.
DR   KEGG; sha:SH0696; -.
DR   eggNOG; COG3850; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OMA; ANDLLWW; -.
DR   OrthoDB; 1827824at2; -.
DR   Proteomes; UP000000543; 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..456
FT                   /note="Heme sensor protein HssS"
FT                   /id="PRO_0000331353"
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   456 AA;  52618 MW;  019C677D171C1134 CRC64;
     MFKTLYTRIA IYTITVILFS ALVSFLFANV YYHFNLKAHN DAKIMRTLKE ARAFHTSSNQ
     SDTQSYFKHL GDMNYQIMIV DHSYHKTFFG EPFRKDTISD SAINQVLKGK AYHGIKNKPF
     ELFITGFFDN ETDNTVGIPF NQNNQKLAVF MRPDIGETFS EFRTFLAVLL ICLLGISITL
     VIASTYSIIK PIKILKQATE RLMHGDFNSP IYQSRHDEIG TLQYRFEAMR QSLKQVDDMR
     QHFVQNVSHE IKTPLTHIHR LLSTLQSNVN QGERDQIIHE IHEEVTHLSN LTKELLLLSE
     LDNATHLKFE DDVHFKELIT DIIRHEQYGI DNKQLMLMSD IDTVHFRGNN RLLHQACSNL
     IQNAIKYSNP NSMIDVNLFN NEGTIYFTVT NEGHTIPESV QPHLFDRFYK RNAEDNSNGL
     GLAITQSIIH LHRGQISVTS NDRDGTTFTV TLPETN