HSSS_STAA3
ID HSSS_STAA3 Reviewed; 457 AA.
AC Q2FED4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Heme sensor protein HssS;
DE EC=2.7.13.3;
GN Name=hssS; OrderedLocusNames=SAUSA300_2309;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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; CP000255; ABD20812.1; -; Genomic_DNA.
DR RefSeq; WP_000477329.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FED4; -.
DR SMR; Q2FED4; -.
DR EnsemblBacteria; ABD20812; ABD20812; SAUSA300_2309.
DR KEGG; saa:SAUSA300_2309; -.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OMA; IDNIAHE; -.
DR Proteomes; UP000001939; 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_0000331350"
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; 52375 MW; 3EE4DB5A89F1D627 CRC64;
MFKTLYARIA IYSITVILFS ALISFVLTNV YYHYNLKASN DAKIMKTLKE ARQYEQSAKP
THIQQYFKHL GQMNYQIMTI DQKGHKTFYG EPFREDTLSQ NAINNVLNNQ DYHGIKDKPF
ALFVTGFFDN VTDNTVGINF KTKDGSIAVF MRPDIGETFS EFRTFLAVLL MLLLFISISL
VIASTYSIIR PVKKLKLATE RLIDGDFETP IKQTRKDEIG TLQYHFNKMR ESLGQVDQMR
QHFVQNVSHE IKTPLTHIHH LLSELQQTSD KTLRQQYIND IYTITTQLSG LTTELLLLSE
LDNHQHLLFD DKIQVNQLIK DIIRHEQFAA DEKSLIILAD LESINFLGNQ RLLHQALSNL
LINAIKYTDV GGAIDIALQH SHNNIIFTIS NDGSPISPQA EARLFERFYK VSKHDNSNGL
GLAITKSIIE LHHGTIQFTQ SNEYVTTFTI TLPNNSL