ID   WALK_STAHJ              Reviewed;         608 AA.
AC   Q4LAJ8;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 134.
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=SH0018;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE03327.1; -; Genomic_DNA.
DR   RefSeq; WP_011274376.1; NC_007168.1.
DR   AlphaFoldDB; Q4LAJ8; -.
DR   SMR; Q4LAJ8; -.
DR   STRING; 279808.SH0018; -.
DR   EnsemblBacteria; BAE03327; BAE03327; SH0018.
DR   KEGG; sha:SH0018; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_2_9; -.
DR   OMA; LTFWAVN; -.
DR   OrthoDB; 1827824at2; -.
DR   Proteomes; UP000000543; 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: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; IPR029150; dCache_3.
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; PF14827; dCache_3; 1.
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; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..608
FT                   /note="Sensor protein kinase WalK"
FT                   /id="PRO_0000353067"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          203..255
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          260..330
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          324..377
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          381..599
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         384
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   608 AA;  69926 MW;  B71B8A57BD9BAD64 CRC64;
     MKWLKQLQSL HTKLVIVYVL LIIIGMQIIG LYFTNSLEKE LTNNFMKNIK QYATQLEVNI
     ERIYRDDPSN AQKEVQSLLN EYANRQEIEE IRFIDKDQII MATAKISSHN MINQKVNDNS
     VQKALSLGES NSHNVLKDYG SGKERIWIYN LPVKNGNETI GNIYIESNIN DVYNQLNNIN
     QIFIIGTAIS LFITVILGFF IARTITRPIT DMRNQTVEMS KGNYTQRVKI YGNDEIGELA
     LAFNNLSKRV QEAQANTESE KRRLDSVITH MSDGIIATDR RGRVRIVNDM AIKMLGMSKE
     DLIGYYMLSV LNLEDEFSLD EIQENNDSFL LDINEDEGII ARVNFSTIVQ ETGFVTGYIA
     VLHDVTEQQQ VERERREFVA NVSHELRTPL TSMNSYIEAL EEGVWKDDNL APSFLSVTRE
     ETERMIRLVN DLLQLSKMDN ESEQITKEIV DFNMFINKII NRHEMAAKDT TFVREIPSET
     IFTEIDPDKM TQVFDNVITN AMKYSRGEKR VEFHVKQNAL YNRMTIRIKD NGIGIPINKV
     DKIFDRFYRV DKARTRKMGG TGLGLAISKE IVEAHNGRIW ANSVEGQGTS IFITLPCEVI
     DDGDWDEE