KDPD_STAA8
ID KDPD_STAA8 Reviewed; 885 AA.
AC Q2FWH7;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Sensor histidine kinase KdpD {ECO:0000303|PubMed:20498265};
DE EC=2.7.13.3;
GN Name=kdpD {ECO:0000303|PubMed:20498265}; OrderedLocusNames=SAOUHSC_02314;
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 [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 [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20498265; DOI=10.1128/iai.00131-10;
RA Zhao L., Xue T., Shang F., Sun H., Sun B.;
RT "Staphylococcus aureus AI-2 quorum sensing associates with the KdpDE two-
RT component system to regulate capsular polysaccharide synthesis and
RT virulence.";
RL Infect. Immun. 78:3506-3515(2010).
RN [3]
RP FUNCTION, AND INDUCTION BY AGR.
RX PubMed=21422185; DOI=10.1128/iai.01180-10;
RA Xue T., You Y., Hong D., Sun H., Sun B.;
RT "The Staphylococcus aureus KdpDE two-component system couples extracellular
RT K+ sensing and Agr signaling to infection programming.";
RL Infect. Immun. 79:2154-2167(2011).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=26195599; DOI=10.1128/jb.00480-15;
RA Moscoso J.A., Schramke H., Zhang Y., Tosi T., Dehbi A., Jung K.,
RA Gruendling A.;
RT "Binding of Cyclic Di-AMP to the Staphylococcus aureus Sensor Kinase KdpD
RT Occurs via the Universal Stress Protein Domain and Downregulates the
RT Expression of the Kdp Potassium Transporter.";
RL J. Bacteriol. 198:98-110(2016).
CC -!- FUNCTION: Member of the two-component regulatory system KdpD/KdpE that
CC regulates the transcription of a series of virulence factors through
CC sensing external K(+) concentrations (PubMed:21422185,
CC PubMed:26195599). Regulates also capsular polysaccharide production
CC (PubMed:20498265). May function as a membrane-associated protein kinase
CC that phosphorylates KdpE in response to environmental signals. In turn,
CC KpdE functions as a transcriptional regulator by direct binding to
CC promoter regions of target genes including spa, hla, aur and geh
CC (PubMed:21422185). {ECO:0000269|PubMed:20498265,
CC ECO:0000269|PubMed:21422185, ECO:0000269|PubMed:26195599}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- ACTIVITY REGULATION: Cyclic di-AMP is a negative regulator of the Kdp
CC system. {ECO:0000269|PubMed:26195599}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: By the Agr/RNAIII system. {ECO:0000269|PubMed:21422185}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of kdpD results in decreased
CC transcript level of cap. {ECO:0000269|PubMed:20498265}.
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; CP000253; ABD31348.1; -; Genomic_DNA.
DR RefSeq; WP_000072278.1; NZ_LS483365.1.
DR RefSeq; YP_500793.1; NC_007795.1.
DR PDB; 7JI4; X-ray; 2.30 A; A=213-364.
DR PDBsum; 7JI4; -.
DR AlphaFoldDB; Q2FWH7; -.
DR SMR; Q2FWH7; -.
DR STRING; 1280.SAXN108_2323; -.
DR EnsemblBacteria; ABD31348; ABD31348; SAOUHSC_02314.
DR GeneID; 3920939; -.
DR KEGG; sao:SAOUHSC_02314; -.
DR PATRIC; fig|93061.5.peg.2097; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_113_3_9; -.
DR OMA; LWATAFQ; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.20.120.620; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..885
FT /note="Sensor histidine kinase KdpD"
FT /id="PRO_0000448704"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 660..880
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 663
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:7JI4"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:7JI4"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:7JI4"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:7JI4"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:7JI4"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:7JI4"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:7JI4"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:7JI4"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:7JI4"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:7JI4"
SQ SEQUENCE 885 AA; 102219 MW; 17A0FEFE559BF5BB CRC64;
MSNTESLNIG KKRGSLTIYI GYSPGVGKTF EMLSNAIELF QSNVDIKIGY IEPHQRDETN
ALAEQLPKIT TNFTKHGSHH FQYLDVDRII EESPTIVLID ELAHTNISRD RHEKRYMDIE
EILNHGIDVH TTLNIQHIES LSSQIELMTG VHVKERVPDY FIMSADVLEV VDISPEQLIK
RLKAGKVYKK DRLDVAFSNF FTYAHLSELR TLTLRTVADL MSDKEKVRHN HKTSLKPHIA
VAISGSIYNE AVIKEAFHIA QKEHAKFTAI YIDVFEKNRQ YKDSQKQVHQ HLMLAKSLGA
KVKVVYSQTV ALGLDEWCKN QDVTKLIIGQ HIRNKWRDFF NTPLIDHLMS FEHSYKIEIV
PIKQIPVELK MNKSPYRPKG KRFAIDMLKM ILIQIICVMM GLWIYQLDKH ESSTIILMIF
LIGIILLSIW TRSFIIGFLA AIINVFVFNY FFTEPRYTFE VYRFDYPITF IVSILTSILT
SALLKQIKFQ YSITKKQLYR TDLLFQFNDS IKQTYTVENL LINAGYQINQ LLQQSITIYV
INQSKVIKTI PLQNHIDNTT QQHEQALSWV IKNERQAGAT TDTFPGINKW LIPIGTSPIK
GILAIDYQSS QVINPYDASI LESMLNELSL AVENVTLLKQ TRESMLQAER QLTHSNFLRS
ISHDIRTPLT TIMGNLDILV SHSKDMSIIE KEQLLVHSFQ ESQYLYLLVT NILSLTKLQS
SNVQIKLQPY LVSELVEEID MILERRHLKK RITVSSSVNL QFIHIDSKLI LQALFNLIEN
AVKHTSTDTK INLSIRYASY EQIEFAVIDE GPGISLEEQQ KIFEPFYTGS NKYFKDNQKE
SMGLGLYLVQ TILHKHQSNL QYKPNQPHGS IFYFNIYTDF NEGDV
