SAES_STAEQ
ID SAES_STAEQ Reviewed; 352 AA.
AC Q5HR29;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Histidine protein kinase SaeS;
DE EC=2.7.13.3;
DE AltName: Full=Sensor protein SaeS;
GN Name=saeS; OrderedLocusNames=SERP0364;
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 SaeR/SaeS.
CC Probably functions as a membrane-associated protein kinase that upon
CC sensing the appropriate signal, autophosphorylates and in turn
CC activates the cytosolic response regulator SaeR (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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW53762.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000029; AAW53762.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5HR29; -.
DR SMR; Q5HR29; -.
DR STRING; 176279.SERP0364; -.
DR EnsemblBacteria; AAW53762; AAW53762; SERP0364.
DR KEGG; ser:SERP0364; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_3_9; -.
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; 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; 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.
FT CHAIN 1..352
FT /note="Histidine protein kinase SaeS"
FT /id="PRO_0000295940"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 130..349
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 133
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 352 AA; 40285 MW; 2726104F160739FA CRC64;
MTIFSIRSQI IIGVISSVIL TTIILVIAYK LMWFNGHMTL TLAITTMITS CLTLSICSIF
INPLIQKIKQ FNIKTKQFIN HEKFIDDETF QSPREIKELN DSFNKMAYEI NNQMNMIKNE
QQEKTEIIQN LAHDLKTPLA GIRSYSEGLR DGVISDPQEV HEAYEILIKQ ANRLSILFDD
ITHVINLNTG RSYPLELIQL DQLLVNILQP YEQHIKQENR TLEVNFCTDI DAFYQYRPPI
ERILTNLLDN ALKFSNSGSR IDIIISECKE NDVISISIKD EGIGIVPELQ SRIFERTFRV
EDSRNTKTGG SGLGLYIANE LAQQIDASIT VQSDLDIGTT MTLTLKKFQF KK