KBP_ECOLI
ID KBP_ECOLI Reviewed; 149 AA.
AC P0ADE6; P39169; P76624; P77022; P77023;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Potassium binding protein Kbp {ECO:0000303|PubMed:27112601};
DE Short=K(+) binding protein Kbp {ECO:0000305};
GN Name=kbp {ECO:0000303|PubMed:27112601}; Synonyms=ygaU, yzzM;
GN OrderedLocusNames=b2665, JW2640;
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 PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=25422305; DOI=10.1128/jb.02449-14;
RA Bernal-Cabas M., Ayala J.A., Raivio T.L.;
RT "The Cpx envelope stress response modifies peptidoglycan cross-linking via
RT the L,D-transpeptidase LdtD and the novel protein YgaU.";
RL J. Bacteriol. 197:603-614(2015).
RN [6]
RP STRUCTURE BY NMR, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27112601; DOI=10.1016/j.str.2016.03.017;
RA Ashraf K.U., Josts I., Mosbahi K., Kelly S.M., Byron O., Smith B.O.,
RA Walker D.;
RT "The potassium binding protein Kbp is a cytoplasmic potassium sensor.";
RL Structure 24:741-749(2016).
CC -!- FUNCTION: Highly specific potassium binding protein that is required
CC for normal growth in the presence of high levels of external K(+). May
CC act as a sensor of cytoplasmic K(+) concentration. Binds a single K(+)
CC ion, which induces a large conformational change. Can also bind the
CC larger alkali metal ions Rb(+) and Cs(+), and NH(4)(+)
CC (PubMed:27112601). May be involved in the regulation of peptidoglycan
CC cross-linking (PubMed:25422305). {ECO:0000269|PubMed:25422305,
CC ECO:0000269|PubMed:27112601}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:27112601}.
CC -!- INDUCTION: Transcriptionally regulated by CpxR, which binds directly to
CC the promoter region. {ECO:0000269|PubMed:25422305}.
CC -!- DOMAIN: BON and LysM domains are both required for full K(+) binding.
CC The major K(+) binding site is located in the BON domain and this
CC initial complex is stabilized by interaction with the LysM domain.
CC {ECO:0000269|PubMed:27112601}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant shows retarded growth at high
CC concentrations of K(+) (PubMed:27112601). Deletion of the gene impacts
CC the abundance of muropeptide species. The absence of YgaU leads to the
CC activation of the Cpx pathway (PubMed:25422305).
CC {ECO:0000269|PubMed:25422305, ECO:0000269|PubMed:27112601}.
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DR EMBL; U00096; AAC75712.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16528.1; -; Genomic_DNA.
DR PIR; B65046; B65046.
DR RefSeq; NP_417151.1; NC_000913.3.
DR RefSeq; WP_000522415.1; NZ_STEB01000042.1.
DR PDB; 7PVC; NMR; -; A=1-149.
DR PDBsum; 7PVC; -.
DR AlphaFoldDB; P0ADE6; -.
DR SMR; P0ADE6; -.
DR BioGRID; 4262266; 15.
DR DIP; DIP-48134N; -.
DR IntAct; P0ADE6; 1.
DR STRING; 511145.b2665; -.
DR SWISS-2DPAGE; P0ADE6; -.
DR jPOST; P0ADE6; -.
DR PaxDb; P0ADE6; -.
DR PRIDE; P0ADE6; -.
DR EnsemblBacteria; AAC75712; AAC75712; b2665.
DR EnsemblBacteria; BAA16528; BAA16528; BAA16528.
DR GeneID; 60903599; -.
DR GeneID; 947144; -.
DR KEGG; ecj:JW2640; -.
DR KEGG; eco:b2665; -.
DR PATRIC; fig|511145.12.peg.2757; -.
DR EchoBASE; EB2540; -.
DR eggNOG; COG1652; Bacteria.
DR InParanoid; P0ADE6; -.
DR OMA; AQYHDVV; -.
DR PhylomeDB; P0ADE6; -.
DR BioCyc; EcoCyc:G7395-MON; -.
DR PRO; PR:P0ADE6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030955; F:potassium ion binding; IDA:EcoCyc.
DR GO; GO:0035864; P:response to potassium ion; IMP:EcoCyc.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR007055; BON_dom.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR014004; Transpt-assoc_nodulatn_dom_bac.
DR Pfam; PF04972; BON; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00749; BON; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS50914; BON; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Potassium;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..149
FT /note="Potassium binding protein Kbp"
FT /id="PRO_0000169832"
FT DOMAIN 23..91
FT /note="BON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00229"
FT DOMAIN 97..146
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:7PVC"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:7PVC"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:7PVC"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:7PVC"
FT TURN 41..45
FT /evidence="ECO:0007829|PDB:7PVC"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:7PVC"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:7PVC"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:7PVC"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:7PVC"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:7PVC"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:7PVC"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:7PVC"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:7PVC"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:7PVC"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:7PVC"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:7PVC"
SQ SEQUENCE 149 AA; 16063 MW; DEC6BAF7707DFAE1 CRC64;
MGLFNFVKDA GEKLWDAVTG QHDKDDQAKK VQEHLNKTGI PDADKVNIQI ADGKATVTGD
GLSQEAKEKI LVAVGNISGI ASVDDQVKTA TPATASQFYT VKSGDTLSAI SKQVYGNANL
YNKIFEANKP MLKSPDKIYP GQVLRIPEE
