WALK_STAA8
ID WALK_STAA8 Reviewed; 608 AA.
AC Q2G2U4; Q9XCM6;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, 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 {ECO:0000303|PubMed:17827301}; Synonyms=yycG;
GN OrderedLocusNames=SAOUHSC_00021;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10368139; DOI=10.1128/jb.181.12.3666-3673.1999;
RA Martin P.K., Li T., Sun D., Biek D.P., Schmid M.B.;
RT "Role in cell permeability of an essential two-component system in
RT Staphylococcus aureus.";
RL J. Bacteriol. 181:3666-3673(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP FUNCTION, AND AUTOPHOSPHORYLATION.
RX PubMed=14762013; DOI=10.1128/jb.186.4.1175-1181.2004;
RA Dubrac S., Msadek T.;
RT "Identification of genes controlled by the essential YycG/YycF two-
RT component system of Staphylococcus aureus.";
RL J. Bacteriol. 186:1175-1181(2004).
RN [4]
RP FUNCTION IN REGULATING CELL WALL METABOLISM, BIOFILM FORMATION, AND
RP AUTOLYSIS.
RX PubMed=17827301; DOI=10.1128/jb.00645-07;
RA Dubrac S., Boneca I.G., Poupel O., Msadek T.;
RT "New insights into the WalK/WalR (YycG/YycF) essential signal transduction
RT pathway reveal a major role in controlling cell wall metabolism and biofilm
RT formation in Staphylococcus aureus.";
RL J. Bacteriol. 189:8257-8269(2007).
RN [5]
RP FUNCTION IN VIRULENCE.
RX PubMed=22825451; DOI=10.1128/iai.00195-12;
RA Delaune A., Dubrac S., Blanchet C., Poupel O., Maeder U., Hiron A.,
RA Leduc A., Fitting C., Nicolas P., Cavaillon J.M., Adib-Conquy M.,
RA Msadek T.;
RT "The WalKR system controls major staphylococcal virulence genes and is
RT involved in triggering the host inflammatory response.";
RL Infect. Immun. 80:3438-3453(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 33-182, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=27389096; DOI=10.1016/j.jmb.2016.06.019;
RA Kim T., Choi J., Lee S., Yeo K.J., Cheong H.K., Kim K.K.;
RT "Structural Studies on the Extracellular Domain of Sensor Histidine Kinase
RT YycG from Staphylococcus aureus and Its Functional Implications.";
RL J. Mol. Biol. 428:3074-3089(2016).
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
CC (PubMed:14762013, PubMed:17827301, PubMed:22825451). Functions as a
CC 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 (PubMed:14762013, PubMed:22825451). {ECO:0000269|PubMed:14762013,
CC ECO:0000269|PubMed:17827301, ECO:0000269|PubMed:22825451}.
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 (PubMed:27389096). Forms homooligomers
CC (PubMed:27389096). {ECO:0000269|PubMed:27389096}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27389096};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:14762013}.
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DR EMBL; AF136709; AAD40238.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29210.1; -; Genomic_DNA.
DR RefSeq; WP_000871607.1; NZ_LS483365.1.
DR RefSeq; YP_498627.1; NC_007795.1.
DR PDB; 5IS1; X-ray; 2.00 A; A=33-182.
DR PDB; 7DUD; X-ray; 1.95 A; A/B=35-182.
DR PDBsum; 5IS1; -.
DR PDBsum; 7DUD; -.
DR AlphaFoldDB; Q2G2U4; -.
DR SMR; Q2G2U4; -.
DR STRING; 1280.SAXN108_0021; -.
DR EnsemblBacteria; ABD29210; ABD29210; SAOUHSC_00021.
DR GeneID; 3919192; -.
DR KEGG; sao:SAOUHSC_00021; -.
DR PATRIC; fig|93061.5.peg.19; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_9; -.
DR OMA; LTFWAVN; -.
DR BRENDA; 2.7.13.3; 3352.
DR PHI-base; PHI:7739; -.
DR PRO; PR:Q2G2U4; -.
DR Proteomes; UP000008816; 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:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system; Zinc.
FT CHAIN 1..608
FT /note="Sensor protein kinase WalK"
FT /id="PRO_0000353061"
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"
FT HELIX 37..65
FT /evidence="ECO:0007829|PDB:5IS1"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:5IS1"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:5IS1"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5IS1"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:5IS1"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:5IS1"
FT STRAND 132..156
FT /evidence="ECO:0007829|PDB:5IS1"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:5IS1"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:5IS1"
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
