HDEB_ECOLI
ID HDEB_ECOLI Reviewed; 108 AA.
AC P0AET2; P26605; Q2M7H1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Acid stress chaperone HdeB {ECO:0000255|HAMAP-Rule:MF_00947};
DE AltName: Full=10K-L protein;
DE Flags: Precursor;
GN Name=hdeB {ECO:0000255|HAMAP-Rule:MF_00947}; Synonyms=yhhD, yhiC;
GN OrderedLocusNames=b3509, JW5669;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-49.
RC STRAIN=K12;
RX PubMed=8455549; DOI=10.1007/bf00282791;
RA Yoshida T., Ueguchi C., Yamada H., Mizuno T.;
RT "Function of the Escherichia coli nucleoid protein, H-NS: molecular
RT analysis of a subset of proteins whose expression is enhanced in a hns
RT deletion mutant.";
RL Mol. Gen. Genet. 237:113-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
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 [4]
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 [5]
RP GENE NAME.
RX PubMed=8244952; DOI=10.1128/jb.175.23.7747-7748.1993;
RA Yoshida T., Ueguchi C., Mizuno T.;
RT "Physical map location of a set of Escherichia coli genes (hde) whose
RT expression is affected by the nucleoid protein H-NS.";
RL J. Bacteriol. 175:7747-7748(1993).
RN [6]
RP PROTEIN SEQUENCE OF 30-41.
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 [7]
RP PROTEIN SEQUENCE OF 30-40.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 30-39.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [9]
RP MASS SPECTROMETRY.
RC STRAIN=ATCC 15597;
RX PubMed=12071744; DOI=10.1021/ja025966k;
RA Reid G.E., Shang H., Hogan J.M., Lee G.U., McLuckey S.A.;
RT "Gas-phase concentration, purification, and identification of whole
RT proteins from complex mixtures.";
RL J. Am. Chem. Soc. 124:7353-7362(2002).
RN [10]
RP INDUCTION.
RX PubMed=12399493; DOI=10.1128/jb.184.22.6225-6234.2002;
RA Masuda N., Church G.M.;
RT "Escherichia coli gene expression responsive to levels of the response
RT regulator EvgA.";
RL J. Bacteriol. 184:6225-6234(2002).
RN [11]
RP INDUCTION.
RX PubMed=12657056; DOI=10.1046/j.1365-2958.2003.03428.x;
RA Bordi C., Theraulaz L., Mejean V., Jourlin-Castelli C.;
RT "Anticipating an alkaline stress through the Tor phosphorelay system in
RT Escherichia coli.";
RL Mol. Microbiol. 48:211-223(2003).
RN [12]
RP INDUCTION.
RX PubMed=16204188; DOI=10.1101/gad.1316305;
RA Shin M., Song M., Rhee J.H., Hong Y., Kim Y.J., Seok Y.J., Ha K.S.,
RA Jung S.H., Choy H.E.;
RT "DNA looping-mediated repression by histone-like protein H-NS: specific
RT requirement of Esigma70 as a cofactor for looping.";
RL Genes Dev. 19:2388-2398(2005).
RN [13]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17085547; DOI=10.1128/jb.01522-06;
RA Kern R., Malki A., Abdallah J., Tagourti J., Richarme G.;
RT "Escherichia coli HdeB is an acid stress chaperone.";
RL J. Bacteriol. 189:603-610(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 30-108, SUBUNIT, AND MUTAGENESIS
RP OF 55-TRP-TRP-56.
RX PubMed=22138344; DOI=10.1016/j.jmb.2011.11.026;
RA Wang W., Rasmussen T., Harding A.J., Booth N.A., Booth I.R., Naismith J.H.;
RT "Salt bridges regulate both dimer formation and monomeric flexibility in
RT HdeB and may have a role in periplasmic chaperone function.";
RL J. Mol. Biol. 415:538-546(2012).
CC -!- FUNCTION: Required for optimal acid stress protection, which is
CC important for survival of enteric bacteria in the acidic environment of
CC the host stomach. Exhibits a chaperone-like activity at acidic pH by
CC preventing the aggregation of many different periplasmic proteins.
CC {ECO:0000255|HAMAP-Rule:MF_00947, ECO:0000269|PubMed:17085547}.
CC -!- SUBUNIT: Homodimer at neutral pH. Dissociates into monomers at acidic
CC pH. {ECO:0000269|PubMed:17085547, ECO:0000269|PubMed:22138344}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00947,
CC ECO:0000269|PubMed:17085547}.
CC -!- INDUCTION: Induced by the EvgS/EvgA two-component regulatory system.
CC Negatively regulated by H-NS and the TorS/TorR two-component regulatory
CC system. {ECO:0000269|PubMed:12399493, ECO:0000269|PubMed:12657056,
CC ECO:0000269|PubMed:16204188}.
CC -!- MASS SPECTROMETRY: Mass=9065; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12071744};
CC -!- DISRUPTION PHENOTYPE: Mutants display increased sensitivity to acid
CC stress at pH 2 and pH 3. {ECO:0000269|PubMed:17085547}.
CC -!- MISCELLANEOUS: In vitro, HdeA is more efficient than HdeB at pH 2 and
CC HdeB is more efficient than HdeA at pH 3. In vivo, both are required
CC for optimal protection against acid stress at either pH 3 or pH 2
CC (PubMed:17085547). {ECO:0000305|PubMed:17085547}.
CC -!- SIMILARITY: Belongs to the HdeB family. {ECO:0000255|HAMAP-
CC Rule:MF_00947}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18485.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA01884.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D11109; BAA01884.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00039; AAB18485.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76534.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77785.1; -; Genomic_DNA.
DR PIR; S30269; S30269.
DR RefSeq; NP_417966.4; NC_000913.3.
DR RefSeq; WP_001298717.1; NZ_STEB01000046.1.
DR PDB; 2MYJ; NMR; -; A/B=30-108.
DR PDB; 2XUV; X-ray; 1.50 A; A/B/C/D=30-108.
DR PDBsum; 2MYJ; -.
DR PDBsum; 2XUV; -.
DR AlphaFoldDB; P0AET2; -.
DR SMR; P0AET2; -.
DR BioGRID; 4261137; 6.
DR DIP; DIP-47949N; -.
DR IntAct; P0AET2; 3.
DR STRING; 511145.b3509; -.
DR iPTMnet; P0AET2; -.
DR SWISS-2DPAGE; P0AET2; -.
DR jPOST; P0AET2; -.
DR PaxDb; P0AET2; -.
DR PRIDE; P0AET2; -.
DR EnsemblBacteria; AAC76534; AAC76534; b3509.
DR EnsemblBacteria; BAE77785; BAE77785; BAE77785.
DR GeneID; 58463707; -.
DR GeneID; 948026; -.
DR KEGG; ecj:JW5669; -.
DR KEGG; eco:b3509; -.
DR PATRIC; fig|511145.12.peg.3616; -.
DR EchoBASE; EB1371; -.
DR eggNOG; ENOG50334GK; Bacteria.
DR HOGENOM; CLU_149189_1_0_6; -.
DR OMA; VAFWMLN; -.
DR PhylomeDB; P0AET2; -.
DR BioCyc; EcoCyc:EG11399-MON; -.
DR EvolutionaryTrace; P0AET2; -.
DR PRO; PR:P0AET2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0051082; F:unfolded protein binding; IDA:EcoCyc.
DR GO; GO:1990451; P:cellular stress response to acidic pH; IEA:UniProtKB-UniRule.
DR GO; GO:0010447; P:response to acidic pH; IDA:EcoCyc.
DR Gene3D; 1.10.890.10; -; 1.
DR HAMAP; MF_00947; HdeB; 1.
DR InterPro; IPR038303; HdeA/HdeB_sf.
DR InterPro; IPR028623; HdeB.
DR InterPro; IPR010486; HNS-dep_expression_A/B.
DR Pfam; PF06411; HdeA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Direct protein sequencing; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00947,
FT ECO:0000269|PubMed:8455549, ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9868784, ECO:0000269|Ref.7"
FT CHAIN 30..108
FT /note="Acid stress chaperone HdeB"
FT /id="PRO_0000021405"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 55..56
FT /note="WW->AA: Folded, but does not form homodimers at pH
FT 7."
FT /evidence="ECO:0000269|PubMed:22138344"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:2XUV"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:2XUV"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:2XUV"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2MYJ"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:2XUV"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:2XUV"
SQ SEQUENCE 108 AA; 12043 MW; 4E80163ACFD1399F CRC64;
MNISSLRKAF IFMGAVAALS LVNAQSALAA NESAKDMTCQ EFIDLNPKAM TPVAWWMLHE
ETVYKGGDTV TLNETDLTQI PKVIEYCKKN PQKNLYTFKN QASNDLPN
