ID   HSSS_STAS1              Reviewed;         460 AA.
AC   Q49ZT9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Heme sensor protein HssS;
DE            EC=2.7.13.3;
GN   Name=hssS; OrderedLocusNames=SSP0540;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE17685.1; -; Genomic_DNA.
DR   RefSeq; WP_011302492.1; NZ_MTGA01000036.1.
DR   AlphaFoldDB; Q49ZT9; -.
DR   SMR; Q49ZT9; -.
DR   STRING; 342451.SSP0540; -.
DR   EnsemblBacteria; BAE17685; BAE17685; SSP0540.
DR   KEGG; ssp:SSP0540; -.
DR   PATRIC; fig|342451.11.peg.544; -.
DR   eggNOG; COG3850; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OMA; ANDLLWW; -.
DR   OrthoDB; 1827824at2; -.
DR   Proteomes; UP000006371; 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; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system; Virulence.
FT   CHAIN           1..460
FT                   /note="Heme sensor protein HssS"
FT                   /id="PRO_0000331354"
FT   TRANSMEM        11..31
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   460 AA;  52772 MW;  4D5F4B6636ACDB29 CRC64;
     MFKSLYTRIA IYTITVMIFS AVASFLCTNI IYHNYLKENN DAKIMRTLKD SIQYQKESRI
     EASAPFFKHL GEMNYQVMTI SEDGHRTYYG TEFRKDNISK KTAESVLHGK DYHGIKNLPY
     NPIITGFFEN TTKNTVGIAY QSKGHTYAVF MRPDIGKTFS EFRIFLAILI TLLLLFSIIL
     VISSTYAIIK PIQQLKRATE RLMHGNFDEV IHVTRKDEFG TLQYRFDKMR LSLKQLDDMR
     QHFVQNVSHE IKTPLTHIHH LLDLLKFAKT DNAREQYIEE IYEVTTQLSE LTKALLLLSE
     IDNGAHLDFD DDIQLNQLIK KIIRHEQFSA NEKDLIIMSD LETISMNGNE RLLHQAFQNL
     ITNAIKYSTT GGMVDVTLSQ NLETITCTIT DDGQGMSAET QARIFERFYK SSNHDNSNGL
     GLAIAKAIFE LHHGTITVDS EKNAGTTFTI TFKKVPKTIS