ID   HSSS_STAEQ              Reviewed;         451 AA.
AC   Q5HLN1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Heme sensor protein HssS;
DE            EC=2.7.13.3;
GN   Name=hssS; OrderedLocusNames=SERP1954;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000029; AAW52836.1; -; Genomic_DNA.
DR   RefSeq; WP_001832894.1; NC_002976.3.
DR   AlphaFoldDB; Q5HLN1; -.
DR   SMR; Q5HLN1; -.
DR   STRING; 176279.SERP1954; -.
DR   EnsemblBacteria; AAW52836; AAW52836; SERP1954.
DR   GeneID; 50017962; -.
DR   KEGG; ser:SERP1954; -.
DR   eggNOG; COG3850; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OMA; EPQWSAK; -.
DR   OrthoDB; 1827824at2; -.
DR   Proteomes; UP000000531; 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   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
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..451
FT                   /note="Heme sensor protein HssS"
FT                   /id="PRO_0000331352"
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..451
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   451 AA;  52097 MW;  4129844B4D4FE202 CRC64;
     MFKTLYSRIA IYAITVILFS ALMSFLFTNI YYHFHLKASN DAKIMRTLKE AREYERTQKP
     KPLDTYLKHL GQMNYQIMTV NEHGTKHFYG ETFRKNTISQ SAIKKVLNGE DYHGIKNKPY
     AFFVTGFFDN ETDNTVGIQF KTDDGALAVF MRPDIGETFS EFRIFLAVLI TLLLIISISL
     VIASTYSIIK PVTALKNATT RIMKGDFSTP IKQTRHDEIG TLQSRFNTMR QNLGQVDQMR
     QHFVQNVSHE VKTPLTHLQR LLTQLELTQN EEEKQLCINE MFEITNQVSE LTKELLLLSE
     LDNASHLTFN DNVHLNTLIK DIIRHEQFRT DEKDLVMFTE LEDLYFRGNE RLLHQAFNNL
     IINAMNYAPQ NSMINITLTS TNHLIIFNIE NDGSIAEEDA KHIFDRFYKL SDESSSNGLG
     LAITQSIIHL HHGSITLTSD DKTQFIVKLF I