YPDA_ECOLI
ID YPDA_ECOLI Reviewed; 565 AA.
AC P0AA93; P76523; P76950;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Sensor histidine kinase YpdA {ECO:0000305};
DE EC=2.7.13.3;
GN Name=ypdA; OrderedLocusNames=b2380, JW5388;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF HIS-371.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23222720; DOI=10.1128/jb.02051-12;
RA Fried L., Behr S., Jung K.;
RT "Identification of a target gene and activating stimulus for the YpdA/YpdB
RT histidine kinase/response regulator system in Escherichia coli.";
RL J. Bacteriol. 195:807-815(2013).
RN [6]
RP FUNCTION, AND INTERACTION WITH BTST AND YHJX.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24659770; DOI=10.1128/jb.01554-14;
RA Behr S., Fried L., Jung K.;
RT "Identification of a novel nutrient-sensing histidine kinase/response
RT regulator network in Escherichia coli.";
RL J. Bacteriol. 196:2023-2029(2014).
CC -!- FUNCTION: Member of the two-component regulatory system YpdA/YpdB,
CC which is part of a nutrient-sensing regulatory network composed of
CC YpdA/YpdB, the high-affinity pyruvate signaling system BtsS/BtsR and
CC their respective target proteins, YhjX and BtsT. YpdA activates YpdB by
CC phosphorylation in response to high concentrations of extracellular
CC pyruvate. Activation of the YpdA/YpdB signaling cascade also promotes
CC BtsS/BtsR-mediated btsT expression. {ECO:0000269|PubMed:23222720,
CC ECO:0000269|PubMed:24659770}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with BtsT and YhjX. {ECO:0000269|PubMed:24659770}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR EMBL; U00096; AAC75439.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16250.2; -; Genomic_DNA.
DR PIR; A65012; A65012.
DR RefSeq; NP_416881.1; NC_000913.3.
DR RefSeq; WP_000544359.1; NZ_STEB01000008.1.
DR AlphaFoldDB; P0AA93; -.
DR SMR; P0AA93; -.
DR BioGRID; 4260545; 186.
DR STRING; 511145.b2380; -.
DR jPOST; P0AA93; -.
DR PaxDb; P0AA93; -.
DR PRIDE; P0AA93; -.
DR EnsemblBacteria; AAC75439; AAC75439; b2380.
DR EnsemblBacteria; BAA16250; BAA16250; BAA16250.
DR GeneID; 66673749; -.
DR GeneID; 946723; -.
DR KEGG; ecj:JW5388; -.
DR KEGG; eco:b2380; -.
DR PATRIC; fig|1411691.4.peg.4348; -.
DR EchoBASE; EB3900; -.
DR eggNOG; COG3275; Bacteria.
DR HOGENOM; CLU_020473_3_3_6; -.
DR InParanoid; P0AA93; -.
DR OMA; RVARNEM; -.
DR PhylomeDB; P0AA93; -.
DR BioCyc; EcoCyc:G7243-MON; -.
DR BioCyc; MetaCyc:G7243-MON; -.
DR PRO; PR:P0AA93; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IMP:EcoCyc.
DR GO; GO:0004673; F:protein histidine kinase activity; IMP:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR GO; GO:0031670; P:cellular response to nutrient; IMP:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IMP:EcoCyc.
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 1: Evidence at protein level;
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_0000201338"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..45
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..107
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..172
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
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"
FT MUTAGEN 371
FT /note="H->Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:23222720"
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
