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Hemolysin expression-modulating protein Hha

 HHA_ECOLI               Reviewed;          72 AA.
P0ACE3; P23870; P77120; Q2MBW7;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
22-NOV-2005, sequence version 1.
20-JUN-2018, entry version 97.
RecName: Full=Hemolysin expression-modulating protein Hha;
Name=hha; OrderedLocusNames=b0460, JW0449;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN HEMOLYSIN PRODUCTION,
AND DISRUPTION PHENOTYPE.
STRAIN=K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
PubMed=1956303; DOI=10.1111/j.1365-2958.1991.tb01902.x;
Nieto J.M., Carmona M., Bolland S., Jubete Y., de la Cruz F.,
Juarez A.;
"The hha gene modulates haemolysin expression in Escherichia coli.";
Mol. Microbiol. 5:1285-1293(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
SIMILARITY TO YMOA.
PubMed=1484495; DOI=10.1111/j.1365-2958.1992.tb02214.x;
de la Cruz F., Carmona M., Juarez A.;
"The Hha protein from Escherichia coli is highly homologous to the
YmoA protein from Yersinia enterocolitica.";
Mol. Microbiol. 6:3451-3452(1992).
[6]
FUNCTION, AND FUNCTION IN Y.ENTEROCOLITICA.
STRAIN=K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
PubMed=8145648; DOI=10.1111/j.1365-2958.1994.tb00291.x;
Mikulskis A.V., Cornelis G.R.;
"A new class of proteins regulating gene expression in
enterobacteria.";
Mol. Microbiol. 11:77-86(1994).
[7]
DISRUPTION PHENOTYPE.
STRAIN=5K;
PubMed=10322001;
Balsalobre C., Johansson J., Uhlin B.E., Juarez A., Munoa F.J.;
"Alterations in protein expression caused by the hha mutation in
Escherichia coli: influence of growth medium osmolarity.";
J. Bacteriol. 181:3018-3024(1999).
[8]
FUNCTION IN REGULATION OF THE HEMOLYSIN OPERON, DNA-BINDING, AND
INTERACTION WITH H-NS.
PubMed=10778755; DOI=10.1007/s004380051178;
Nieto J.M., Madrid C., Prenafeta A., Miquelay E., Balsalobre C.,
Carrascal M., Juarez A.;
"Expression of the hemolysin operon in Escherichia coli is modulated
by a nucleoid-protein complex that includes the proteins Hha and H-
NS.";
Mol. Gen. Genet. 263:349-358(2000).
[9]
FUNCTION, INTERACTION WITH H-NS, DOMAIN, AND MUTAGENESIS OF ARG-16;
44-TYR--ARG-72; ARG-50; 58-LYS--ARG-72; PRO-64 AND ARG-72.
PubMed=11790731; DOI=10.1128/JB.184.3.629-635.2002;
Nieto J.M., Madrid C., Miquelay E., Parra J.L., Rodriguez S.,
Juarez A.;
"Evidence for direct protein-protein interaction between members of
the enterobacterial Hha/YmoA and H-NS families of proteins.";
J. Bacteriol. 184:629-635(2002).
[10]
INDUCTION.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=14727089; DOI=10.1007/s00253-003-1517-y;
Ren D., Bedzyk L.A., Thomas S.M., Ye R.W., Wood T.K.;
"Gene expression in Escherichia coli biofilms.";
Appl. Microbiol. Biotechnol. 64:515-524(2004).
[11]
FUNCTION IN BIOFILM FORMATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
PubMed=16317765; DOI=10.1002/bit.20681;
Barrios A.F., Zuo R., Ren D., Wood T.K.;
"Hha, YbaJ, and OmpA regulate Escherichia coli K12 biofilm formation
and conjugation plasmids abolish motility.";
Biotechnol. Bioeng. 93:188-200(2006).
[12]
SUBUNIT.
PubMed=16650431; DOI=10.1016/j.jmb.2006.03.059;
Garcia J., Madrid C., Juarez A., Pons M.;
"New roles for key residues in helices H1 and H2 of the Escherichia
coli H-NS N-terminal domain: H-NS dimer stabilization and Hha
binding.";
J. Mol. Biol. 359:679-689(2006).
[13]
FUNCTION IN BIOFILM FORMATION, INDUCTION, AND DNA-BINDING.
STRAIN=K12 / BW25113;
PubMed=18545668; DOI=10.1371/journal.pone.0002394;
Garcia-Contreras R., Zhang X.S., Kim Y., Wood T.K.;
"Protein translation and cell death: the role of rare tRNAs in biofilm
formation and in activating dormant phage killer genes.";
PLoS ONE 3:E2394-E2394(2008).
[14]
FUNCTION IN PERSISTER CELL FORMATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / BW25113;
PubMed=19909729; DOI=10.1016/j.bbrc.2009.11.033;
Kim Y., Wood T.K.;
"Toxins Hha and CspD and small RNA regulator Hfq are involved in
persister cell formation through MqsR in Escherichia coli.";
Biochem. Biophys. Res. Commun. 391:209-213(2010).
[15]
FUNCTION IN REGULATION OF THE HEMOLYSIN OPERON, INTERACTION WITH H-NS,
AND MUTAGENESIS OF ASP-10; ASP-22; GLU-25; GLU-29; GLU-34; ASP-37;
GLU-39; ASP-48 AND ASP-61.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=21600204; DOI=10.1016/j.febslet.2011.05.024;
de Alba C.F., Solorzano C., Paytubi S., Madrid C., Juarez A.,
Garcia J., Pons M.;
"Essential residues in the H-NS binding site of Hha, a co-regulator of
horizontally acquired genes in Enterobacteria.";
FEBS Lett. 585:1765-1770(2011).
[16]
FUNCTION, REGULON, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=23543115; DOI=10.1093/dnares/dst008;
Ueda T., Takahashi H., Uyar E., Ishikawa S., Ogasawara N., Oshima T.;
"Functions of the Hha and YdgT proteins in transcriptional silencing
by the nucleoid proteins, H-NS and StpA, in Escherichia coli.";
DNA Res. 20:263-271(2013).
[17]
STRUCTURE BY NMR.
PubMed=11854485; DOI=10.1073/pnas.042684599;
Yee A., Chang X., Pineda-Lucena A., Wu B., Semesi A., Le B.,
Ramelot T., Lee G.M., Bhattacharyya S., Gutierrez P., Denisov A.,
Lee C.-H., Cort J.R., Kozlov G., Liao J., Finak G., Chen L.,
Wishart D., Lee W., McIntosh L.P., Gehring K., Kennedy M.A.,
Edwards A.M., Arrowsmith C.H.;
"An NMR approach to structural proteomics.";
Proc. Natl. Acad. Sci. U.S.A. 99:1825-1830(2002).
[18]
STRUCTURE BY NMR IN COMPLEX WITH H-NS, AND SUBUNIT.
PubMed=26085102; DOI=10.1074/jbc.M114.630400;
Cordeiro T.N., Garcia J., Bernado P., Millet O., Pons M.;
"A three-protein charge zipper stabilizes a complex modulating
bacterial gene silencing.";
J. Biol. Chem. 290:21200-21212(2015).
-!- FUNCTION: Down-regulates hemolysin (hly) expression in complex
with H-NS (PubMed:1956303, PubMed:10778755, PubMed:11790731,
PubMed:21600204). Stimulates transposition events in vivo
(PubMed:8145648). Modifies the set of genes regulated by H-NS; Hha
and Cnu (YdgT) increase the number of genes DNA bound by H-NS/StpA
and may also modulate the oligomerization of the H-NS/StpA-complex
(PubMed:23543115). Binds DNA and influences DNA topology in
response to environmental stimuli; does not however interact with
DNA in the absence of H-NS (PubMed:23543115). Involved in
persister cell formation, acting downstream of mRNA interferase
(toxin) MqsR (PubMed:19909729). Decreases biofilm formation by
repressing the transcription of fimbrial genes fimA and ihfA, and
by repressing the transcription of tRNAs corresponding to rare
codons, which are abundant in type 1 fimbrial genes
(PubMed:18545668). {ECO:0000269|PubMed:10778755,
ECO:0000269|PubMed:11790731, ECO:0000269|PubMed:16317765,
ECO:0000269|PubMed:18545668, ECO:0000269|PubMed:1956303,
ECO:0000269|PubMed:19909729, ECO:0000269|PubMed:21600204,
ECO:0000269|PubMed:23543115, ECO:0000269|PubMed:8145648}.
-!- SUBUNIT: Forms a heterotrimeric complex with the H-NS dimer in the
absence of DNA. {ECO:0000269|PubMed:10778755,
ECO:0000269|PubMed:11790731, ECO:0000269|PubMed:16650431,
ECO:0000269|PubMed:21600204, ECO:0000269|PubMed:26085102}.
-!- INTERACTION:
P0ACF8:hns; NbExp=5; IntAct=EBI-1122578, EBI-544934;
-!- INDUCTION: Expression is autoregulated (Probable). Induced during
biofilm formation (PubMed:14727089, PubMed:18545668).
{ECO:0000269|PubMed:14727089, ECO:0000269|PubMed:18545668,
ECO:0000305}.
-!- DOMAIN: Histidine-tagging (His-tagging) at the N-terminus does not
impair interaction with H-NS, whereas His-tagging at the C-
terminus does impair interaction (PubMed:11790731).
{ECO:0000269|PubMed:11790731}.
-!- DISRUPTION PHENOTYPE: Deletion results in a large increase in the
production of extracellular and intracellular hemolysin
(PubMed:1956303). At low osmolarity minor changes in overall
translation, at 0.4 M NaCl expression of about 25 proteins
altered, including decreased OmpA, crr and AhpC (in strain 5K, not
a K12 derivative) (PubMed:10322001). At 0.3 M NaCl in strain W3110
up-regulation of 113 genes and down-regulation of 8 genes was
observed; a double cnu-hha deletion up-regulated 134 and down-
regulated 5 genes, most of which are thought to have been acquired
horizontally and are also up-regulated in double hns-stpA
deletions (PubMed:23543115). However there are only 12 genes that
were commonly up-regulated in the hha and cnu-hha deletions
(PubMed:23543115). Represses the production of persister cells
(PubMed:19909729). Deletion of hha and tomB (ybaJ), in the
presence of a conjugative plasmid (R1drd19), decreases biofilm
formation, cell aggregation and increases motility via flagella
and motility gene expression (PubMed:16317765).
{ECO:0000269|PubMed:10322001, ECO:0000269|PubMed:16317765,
ECO:0000269|PubMed:1956303, ECO:0000269|PubMed:19909729,
ECO:0000269|PubMed:23543115}.
-!- MISCELLANEOUS: Hha and TomB may form a type II toxin-antitoxin
(TA) system (PubMed:18545668). {ECO:0000305|PubMed:18545668}.
-!- SIMILARITY: Belongs to the Hha/YmoA/Cnu family.
{ECO:0000305|PubMed:1484495, ECO:0000305|PubMed:8145648}.
-!- SEQUENCE CAUTION:
Sequence=AAB40215.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X57977; CAA41043.1; -; Genomic_DNA.
EMBL; U82664; AAB40215.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC73562.1; -; Genomic_DNA.
EMBL; AP009048; BAE76239.1; -; Genomic_DNA.
PIR; C64776; C64776.
RefSeq; NP_414993.1; NC_000913.3.
RefSeq; WP_001291435.1; NZ_LN832404.1.
PDB; 1JW2; NMR; -; A=1-72.
PDB; 2MW2; NMR; -; A=1-72.
PDBsum; 1JW2; -.
PDBsum; 2MW2; -.
ProteinModelPortal; P0ACE3; -.
SMR; P0ACE3; -.
BioGrid; 4262034; 9.
ComplexPortal; CPX-1979; H-NS-Hha complex.
DIP; DIP-9897N; -.
IntAct; P0ACE3; 2.
MINT; P0ACE3; -.
STRING; 316385.ECDH10B_0416; -.
PaxDb; P0ACE3; -.
PRIDE; P0ACE3; -.
EnsemblBacteria; AAC73562; AAC73562; b0460.
EnsemblBacteria; BAE76239; BAE76239; BAE76239.
GeneID; 945098; -.
KEGG; ecj:JW0449; -.
KEGG; eco:b0460; -.
PATRIC; fig|511145.12.peg.478; -.
EchoBASE; EB0434; -.
EcoGene; EG10439; hha.
eggNOG; ENOG4105KF5; Bacteria.
eggNOG; ENOG4111U15; LUCA.
HOGENOM; HOG000219358; -.
KO; K05839; -.
OMA; RRCQSID; -.
BioCyc; EcoCyc:EG10439-MONOMER; -.
EvolutionaryTrace; P0ACE3; -.
PRO; PR:P0ACE3; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0010468; P:regulation of gene expression; IMP:EcoCyc.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.1280.40; -; 1.
InterPro; IPR007985; Hemolysn_expr_modulating_HHA.
InterPro; IPR036666; HHA_sf.
Pfam; PF05321; HHA; 1.
SUPFAM; SSF68989; SSF68989; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Reference proteome; Repressor;
Transcription; Transcription regulation.
CHAIN 1 72 Hemolysin expression-modulating protein
Hha.
/FTId=PRO_0000201727.
SITE 25 25 Interacts with H-NS.
SITE 48 48 Interacts with H-NS.
MUTAGEN 10 10 D->N: Does not affect H-NS binding
ability. {ECO:0000269|PubMed:21600204}.
MUTAGEN 16 16 R->C: Derepression of the hly operon,
impaired H-NS binding.
{ECO:0000269|PubMed:11790731}.
MUTAGEN 22 22 D->N: Does not affect H-NS binding
ability. {ECO:0000269|PubMed:21600204}.
MUTAGEN 25 25 E->Q: Affects H-NS binding ability.
Decrease in the ability to repress the
expression of the hly operon.
{ECO:0000269|PubMed:21600204}.
MUTAGEN 29 29 E->Q: Does not affect H-NS binding
ability. {ECO:0000269|PubMed:21600204}.
MUTAGEN 34 34 E->Q: Does not affect H-NS binding
ability. {ECO:0000269|PubMed:21600204}.
MUTAGEN 37 37 D->N: Does not affect H-NS binding
ability. {ECO:0000269|PubMed:21600204}.
MUTAGEN 39 39 E->Q: Does not affect H-NS binding
ability. {ECO:0000269|PubMed:21600204}.
MUTAGEN 44 72 Missing: Derepression of the hly operon,
impaired H-NS binding.
{ECO:0000269|PubMed:11790731}.
MUTAGEN 48 48 D->E,R: Abolishes the interaction with H-
NS. {ECO:0000269|PubMed:21600204}.
MUTAGEN 48 48 D->N: Abolishes the interaction with H-
NS. Loss of the ability to repress the
expression of the hly operon.
{ECO:0000269|PubMed:21600204}.
MUTAGEN 50 50 R->H: Derepression of the hly operon,
impaired H-NS binding.
{ECO:0000269|PubMed:11790731}.
MUTAGEN 58 72 Missing: Derepression of the hly operon,
impaired H-NS binding.
{ECO:0000269|PubMed:11790731}.
MUTAGEN 61 61 D->N: Does not affect H-NS binding
ability. {ECO:0000269|PubMed:21600204}.
MUTAGEN 64 64 P->L,S: Derepression of the hly operon,
impaired H-NS binding.
{ECO:0000269|PubMed:11790731}.
MUTAGEN 72 72 R->RHHHHHH: Derepression of the hly
operon, impaired H-NS binding.
{ECO:0000269|PubMed:11790731}.
HELIX 8 16 {ECO:0000244|PDB:1JW2}.
HELIX 21 34 {ECO:0000244|PDB:1JW2}.
HELIX 37 55 {ECO:0000244|PDB:1JW2}.
STRAND 56 58 {ECO:0000244|PDB:1JW2}.
HELIX 65 70 {ECO:0000244|PDB:1JW2}.
SEQUENCE 72 AA; 8628 MW; A77211B87CF0134A CRC64;
MSEKPLTKTD YLMRLRRCQT IDTLERVIEK NKYELSDNEL AVFYSAADHR LAELTMNKLY
DKIPSSVWKF IR


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