WALK_STAEQ
ID WALK_STAEQ Reviewed; 610 AA.
AC Q5HK19;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=SERP2533;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP FUNCTION IN REGULATING CELL WALL METABOLISM AND BIOFILM FORMATION.
RX PubMed=17094812; DOI=10.1186/1471-2180-6-96;
RA Qin Z.-Q., Zhang J., Xu B., Chen L., Wu Y., Yang X., Shen X., Molin S.,
RA Danchin A., Jiang H., Qu D.;
RT "Structure-based discovery of inhibitors of the YycG histidine kinase: new
RT chemical leads to combat Staphylococcus epidermidis infections.";
RL BMC Microbiol. 6:96-96(2006).
CC -!- FUNCTION: Member of the two-component regulatory system WalK/WalR that
CC regulates genes involved in autolysis, biofilm formation and cell wall
CC metabolism. WalK functions as a sensor protein kinase which is
CC autophosphorylated at a histidine residue and transfers its phosphate
CC group to WalR. {ECO:0000250|UniProtKB:Q2G2U4,
CC ECO:0000269|PubMed:17094812}.
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; CP000029; AAW53341.1; -; Genomic_DNA.
DR RefSeq; WP_002437327.1; NC_002976.3.
DR AlphaFoldDB; Q5HK19; -.
DR SMR; Q5HK19; -.
DR STRING; 176279.SERP2533; -.
DR BindingDB; Q5HK19; -.
DR ChEMBL; CHEMBL4295848; -.
DR EnsemblBacteria; AAW53341; AAW53341; SERP2533.
DR GeneID; 50017435; -.
DR KEGG; ser:SERP2533; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_9; -.
DR OMA; LTFWAVN; -.
DR OrthoDB; 1827824at2; -.
DR Proteomes; UP000000531; 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; 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; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..610
FT /note="Sensor protein kinase WalK"
FT /id="PRO_0000353066"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 206..258
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 263..334
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 327..380
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 384..602
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 387
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 610 AA; 69944 MW; 1ECE9A660C6EF6D9 CRC64;
MKWLKQLQSL HTKLVIVYVL LIIIGMQIIG LYFTNSLEKE LLDNFKKNIT QYAKQLDVNI
EKVYKDKDKG SVNAQKDIQD LLNEYANRQE IGEIRFIDKD QIIMATTKQS NRGLINQKVN
DGSVQKALSL GQTNDHMVLK DYGSGKERVW VYNIPVKVDK QTIGDIYIES KINDVYNQLN
NINQIFIVGT AISLFITVIL GFFIARTITK PITDMRNQTV EMSKGNYTQR VKIYGNDEIG
ELALAFNNLS KRVQEAQANT ESEKRRLDSV ITHMSDGILA TDRRGRVRIA NDMALKMLGL
AKEDVIGYYM LGVLNLENEF SLEEIQENSD SFLLDINEEE GIIARVNFST IVQETGFVTG
YIAVLHDVTE QQQVERERRE FVANVSHELR TPLTSMNSYI EALEEGAWQD KELAPSFLSV
TREETERMIR LVNDLLQLSK MDNESDQITK EIIDFNMFIN KIINRHEMAA KDTTFVREIP
QQTIFAEIDP DKMTQVFDNV ITNAMKYSRG EKRVEFHVKQ NALYNRMTIR IKDNGIGIPI
NKVDKIFDRF YRVDKARTRK MGGTGLGLAI SKEIVEAHNG RIWANSVEGQ GTSIFITLPC
EIIEDGDWDE
