ID   WALK_MAMSC              Reviewed;         419 AA.
AC   A5A2P0;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Sensor protein kinase WalK {ECO:0000305};
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:O34206};
DE   Flags: Fragment;
GN   Name=walK; Synonyms=yycG;
OS   Mammaliicoccus sciuri (Staphylococcus sciuri).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Mammaliicoccus.
OX   NCBI_TaxID=1296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Subsp. rodentium / K3;
RA   Zhou Y., Wu S.W., Tomasz A.;
RT   "Further study on strains of Staphylococcus sciuri carrying mecA of
RT   Staphylococcus aureus: scrutinizing effect of antibiotic pressure on
RT   bacterial phenotype and genotype and revealing wide variation in vicinities
RT   of OrfX and mecA of Staphylococcus sciuri.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Member of the two-component regulatory system WalK/WalR. WalK
CC       functions as a sensor protein kinase which is autophosphorylated at a
CC       histidine residue and transfers its phosphate group to WalR.
CC       {ECO:0000250|UniProtKB:Q2G2U4}.
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:O34206};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q2G2U4}.
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DR   EMBL; EF521823; ABP68577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5A2P0; -.
DR   SMR; A5A2P0; -.
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   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; IPR035965; PAS-like_dom_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; PF13426; PAS_9; 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; 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; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane;
KW   Two-component regulatory system.
FT   CHAIN           <1..419
FT                   /note="Sensor protein kinase WalK"
FT                   /id="PRO_0000353069"
FT   DOMAIN          11..63
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          68..138
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          132..185
FT                   /note="PAC"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          189..409
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         192
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   NON_TER         1
SQ   SEQUENCE   419 AA;  47917 MW;  92D2979BC0D1A303 CRC64;
     ITIVLGFFIA RTITKPISDM RNQTLEMSKG NYTQRVKIYG NDEIGELALS FNNLSKRVQE
     AQANTESEKR RLDSVITHMS DGVLATDRRG RVRIINEMAL KMLGLECADV EAKHILDILN
     IDDDYSLDDL QENNDSFIID INSEEGIIAR VNFSTIIQDT GFINGYIAVL HDVTEQHILE
     NERREFVANV SHELRTPLTS MRSYIEALEE GAWRDPEVAP TFLNVTREET DRMIRLVNDL
     LQLSKMDSSS DQMNSELINF NMFINKIINR HEMSQGKNVT FIRDIPVKGL FVEIDPDKMT
     QVFDNVITNA IKYSQESHKR VEFHVKQNTL YNRMTIQIKD NGIGIPVNKV DKIFDRFYRV
     DKARARKMGG TGLGLAITKE IVEAHKGRIW ASSKEGQGTS IYITLPCEVM EDEFGDWDA