WALK_STAAB
ID WALK_STAAB Reviewed; 608 AA.
AC Q2YUQ2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Sensor protein kinase WalK {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:O34206};
GN Name=walK; Synonyms=yycG; OrderedLocusNames=SAB0019;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI79707.1; -; Genomic_DNA.
DR RefSeq; WP_000871607.1; NC_007622.1.
DR AlphaFoldDB; Q2YUQ2; -.
DR SMR; Q2YUQ2; -.
DR KEGG; sab:SAB0019; -.
DR HOGENOM; CLU_000445_89_2_9; -.
DR OMA; LTFWAVN; -.
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_0000353051"
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; 69924 MW; FBE26E64D2A37A8D 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 INRHEMSAKD TTFIRDIPKK
TIFTEFDPDK MTQVFDNVIT NAMKYSRGDK RVEFHVKQNP LYNRMTIRIK DNGIGIPINK
VDKIFDRFYR VDKARTRKMG GTGLGLAISK EIVEAHNGRI WANSVEGQGT SIFITLPCEV
IEDGDWDE
