ID   WALK_STAAR              Reviewed;         608 AA.
AC   Q6GKS6;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Sensor protein kinase WalK {ECO:0000305};
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:O34206};
GN   Name=walK; Synonyms=vicK, yycG; OrderedLocusNames=SAR0019;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Member of the two-component regulatory system WalK/WalR that
CC       regulates genes involved in cell wall metabolism, virulence regulation,
CC       biofilm production, oxidative stress resistance and antibiotic
CC       resistance via direct or indirect regulation of autolysins. Functions
CC       as a sensor protein kinase which is autophosphorylated at a histidine
CC       residue in the dimerization domain and transfers its phosphate group to
CC       the conserved aspartic acid residue in the regulatory domain of WalR.
CC       In turn, WalR binds to the upstream promoter regions of the target
CC       genes to positively and negatively regulate their expression.
CC       {ECO:0000250|UniProtKB:Q9RDT3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:Q9RDT3};
CC   -!- ACTIVITY REGULATION: By zinc. Zinc-binding negatively regulates WalK
CC       kinase activity and thus autophosphorylation.
CC       {ECO:0000250|UniProtKB:Q9RDT3}.
CC   -!- SUBUNIT: Forms homodimers. Forms homooligomers.
CC       {ECO:0000250|UniProtKB:Q2G2U4}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9RDT3}.
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DR   EMBL; BX571856; CAG39047.1; -; Genomic_DNA.
DR   RefSeq; WP_000871610.1; NC_002952.2.
DR   AlphaFoldDB; Q6GKS6; -.
DR   SMR; Q6GKS6; -.
DR   PRIDE; Q6GKS6; -.
DR   KEGG; sar:SAR0019; -.
DR   HOGENOM; CLU_000445_89_2_9; -.
DR   OMA; LTFWAVN; -.
DR   OrthoDB; 1827824at2; -.
DR   Proteomes; UP000000596; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR029151; Sensor-like_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   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF103190; SSF103190; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system; Zinc.
FT   CHAIN           1..608
FT                   /note="Sensor protein kinase WalK"
FT                   /id="PRO_0000353055"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          204..256
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          261..331
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          314..378
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          382..600
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RDT3"
FT   BINDING         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RDT3"
FT   BINDING         364
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RDT3"
FT   BINDING         368
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RDT3"
FT   MOD_RES         385
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   608 AA;  69954 MW;  FBE2756569A3DA8C CRC64;
     MKWLKQLQSL HTKLVIVYVL LIIIGMQIIG LYFTNNLEKE LLDNFKKNIT QYAKQLEISI
     EKVYDEKGSV NAQKDIQNLL SEYANRQEIG EIRFIDKDQI IIATTKQSNR SLINQKANDS
     SVQKALSLGQ SNDHLILKDY GGGKDRVWVY NIPVKVDKKV IGNIYIESKI NDVYNQLNNI
     NQIFIVGTAI SLLITVILGF FIARTITKPI TDMRNQTVEM SRGNYTQRVK IYGNDEIGEL
     ALAFNNLSKR VQEAQANTES EKRRLDSVIT HMSDGIIATD RRGRIRIVND MALKMLGMAK
     EDIIGYYMLS VLSLEDEFKL EEIQENNDSF LLDLNEEEGL IARVNFSTIV QETGFVTGYI
     AVLHDVTEQQ QVERERREFV ANVSHELRTP LTSMNSYIEA LEEGAWKDEE LAPQFLSVTR
     EETERMIRLV NDLLQLSKMD NESDQINKEI IDFNMFINKI INRHEMSTKD TTFIRDIPKK
     TIFTEFDPDK MTQVFDNVIT NAMKYSRGDK RVEFHVKQNP LYNRMTIRIK DNGIGIPINK
     VDKIFDRFYR VDKARTRKMG GTGLGLAISK EIVEAHNGRI WANSVEGQGT SIFITLPCEV
     IEDGDWDE