SAES_STAA3
ID SAES_STAA3 Reviewed; 351 AA.
AC Q2FIT5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Histidine protein kinase SaeS;
DE EC=2.7.13.3;
DE AltName: Full=Sensor protein SaeS;
DE AltName: Full=Staphylococcus exoprotein expression protein S;
GN Name=saeS; OrderedLocusNames=SAUSA300_0690;
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 SaeR/SaeS
CC involved in the regulation of staphylococcal virulence factors in a
CC strain-dependent fashion. Probably functions as a membrane-associated
CC protein kinase that upon sensing the appropriate signal,
CC autophosphorylates and in turn activates the cytosolic response
CC regulator SaeR (By similarity). {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; ABD20913.1; -; Genomic_DNA.
DR RefSeq; WP_000244412.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FIT5; -.
DR SMR; Q2FIT5; -.
DR PRIDE; Q2FIT5; -.
DR EnsemblBacteria; ABD20913; ABD20913; SAUSA300_0690.
DR KEGG; saa:SAUSA300_0690; -.
DR HOGENOM; CLU_000445_89_3_9; -.
DR OMA; LIRVIDH; -.
DR PHI-base; PHI:4224; -.
DR PHI-base; PHI:4683; -.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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..351
FT /note="Histidine protein kinase SaeS"
FT /id="PRO_0000295938"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 61..114
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 129..348
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 132
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 351 AA; 39741 MW; 08CB447C472A1B47 CRC64;
MVLSIRSQII IGVVSSILLT STILAIAYIL MWFNGHMTLT LTLTTIITSC LTLLICSIFI
NPLIQKIKQF NIKTKQFANG NYASNDKTFN SPKEIYELNQ SFNKMASEIT QQMNQIKSEQ
QEKTELIQNL AHDLKTPLAS IISYSEGLRD GIITKDHEIK ESYDILIKQA NRLSTLFDDM
THIITLNTGK TYPPELIQLD QLLVSILQPY EQRIKHENRT LEVNFCNEID AFYQYRTPLE
RILTNLLDNA LKFSNVGSRI DINISENEDQ DTIDIAISDE GIGIIPELQE RIFERTFRVE
NSRNTKTGGS GLGLYIANEL AQQNNAKISV SSDIDVGTTM TVTLHKLDIT S