YPDA_ECO57
ID YPDA_ECO57 Reviewed; 565 AA.
AC P0AA94; P76523; P76950;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Sensor histidine kinase YpdA {ECO:0000250|UniProtKB:P0AA93};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P0AA93};
GN Name=ypdA; OrderedLocusNames=Z3645, ECs3260;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Member of the two-component regulatory system YpdA/YpdB. YpdA
CC activates YpdB by phosphorylation in response to high concentrations of
CC extracellular pyruvate. {ECO:0000250|UniProtKB:P0AA93}.
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:P0AA93};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AA93}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR EMBL; AE005174; AAG57506.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36683.1; -; Genomic_DNA.
DR PIR; D91036; D91036.
DR PIR; F85880; F85880.
DR RefSeq; NP_311287.1; NC_002695.1.
DR RefSeq; WP_000544359.1; NZ_SDVX01000004.1.
DR AlphaFoldDB; P0AA94; -.
DR SMR; P0AA94; -.
DR STRING; 155864.EDL933_3549; -.
DR EnsemblBacteria; AAG57506; AAG57506; Z3645.
DR EnsemblBacteria; BAB36683; BAB36683; ECs_3260.
DR GeneID; 66673749; -.
DR GeneID; 915638; -.
DR KEGG; ece:Z3645; -.
DR KEGG; ecs:ECs_3260; -.
DR PATRIC; fig|386585.9.peg.3404; -.
DR eggNOG; COG3275; Bacteria.
DR HOGENOM; CLU_020473_3_3_6; -.
DR OMA; RVARNEM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0071555; P:cell wall organization; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..565
FT /note="Sensor histidine kinase YpdA"
FT /id="PRO_0000201339"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..44
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 77..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..105
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..168
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 169..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA93"
FT DOMAIN 223..342
FT /note="GAF"
FT DOMAIN 343..554
FT /note="Histidine kinase"
FT MOD_RES 371
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 565 AA; 62657 MW; 1CD1B604BA5E48B1 CRC64;
MHEIFNMLLA VFDRAALMLI CLFFLIRIRL FRELLHKSAH SPKELLAVTA IFSLFALFST
WSGVPVEGSL VNVRIIAVMS GGILFGPWVG IITGVIAGIH RYLIDIGGVT AIPCFITSIL
AGCISGWINL KIPKAQRWRV GILGGMLCET LTMILVIVWA PTTALGIDIV SKIGIPMILG
SVCIGFIVLL VQSVEGEKEA SAARQAKLAL DIANKTLPLF RHVNSESLRK VCEIIRDDIH
ADAVAITNTD HVLAYVGVGE HNYQNGDDFI SPTTRQAMNY GKIIIKNNDE AHRTPEIHSM
LVIPLWEKGV VTGTLKIYYC HAHQITSSLQ EMAVGLSQII STQLEVSRAE QLREMANKAE
LRALQSKINP HFLFNALNAI SSSIRLNPDT ARQLIFNLSR YLRYNIELKD DEQIDIKKEL
YQIKDYIAIE QARFGDKLTV IYDIDEEVNC CIPSLLIQPL VENAIVHGIQ PCKGKGVVTI
SVAECGNRVR IAVRDTGHGI DPKVIERVEA NEMPGNKIGL LNVHHRVKLL YGEGLHIRRL
EPGTEIAFYI PNQRTPVASQ ATLLL
