WALK_STAAN
ID WALK_STAAN Reviewed; 608 AA.
AC Q7A8E0;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Sensor protein kinase WalK {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:O34206};
GN Name=walK; Synonyms=vicK; OrderedLocusNames=SA0018;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
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:0000269|PubMed:20713508};
CC Multi-pass membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000269|PubMed:20713508}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Present in detergent-resistant membrane (DRM)
CC fractions that may be equivalent to eukaryotic membrane rafts; these
CC rafts include proteins involved in signaling, molecule trafficking and
CC protein secretion. {ECO:0000269|PubMed:20713508}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9RDT3}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000018; BAB41235.1; -; Genomic_DNA.
DR PIR; C89760; C89760.
DR RefSeq; WP_000871607.1; NC_002745.2.
DR AlphaFoldDB; Q7A8E0; -.
DR SMR; Q7A8E0; -.
DR EnsemblBacteria; BAB41235; BAB41235; BAB41235.
DR KEGG; sau:SA0018; -.
DR HOGENOM; CLU_000445_89_2_9; -.
DR OMA; LTFWAVN; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
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_0000353060"
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
