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HHA_SALTY
ID   HHA_SALTY               Reviewed;          72 AA.
AC   Q7CR17; Q7BLT0;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Hemolysin expression-modulating protein Hha;
GN   Name=hha; OrderedLocusNames=STM0473;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) IN COMPLEX WITH H-NS N-TERMINAL
RP   FRAGMENT, FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   14-ARG--ARG-17; ARG-14; ARG-17; ARG-26 AND ASP-48.
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=23515315; DOI=10.1074/jbc.m113.455378;
RA   Ali S.S., Whitney J.C., Stevenson J., Robinson H., Howell P.L.,
RA   Navarre W.W.;
RT   "Structural insights into the regulation of foreign genes in Salmonella by
RT   the Hha/H-NS complex.";
RL   J. Biol. Chem. 288:13356-13369(2013).
CC   -!- FUNCTION: Interacts with H-NS and in this complex might contact DNA,
CC       which could provide an additional surface for DNA binding to the H-NS-
CC       Hha complex; may not bind DNA in the absence of H-NS (PubMed:23515315).
CC       In vitro improves the ability of H-NS to bind DNA under a precise set
CC       of conditions (PubMed:23515315). {ECO:0000269|PubMed:23515315}.
CC   -!- SUBUNIT: Interacts with H-NS; crystal structures suggest each subunit
CC       of an H-NS dimer could bind 1 Hha monomer (PubMed:23515315).
CC       {ECO:0000269|PubMed:23515315}.
CC   -!- DISRUPTION PHENOTYPE: Derepression of genes that are usually
CC       coregulated by H-NS and Hha (PubMed:23515315).
CC       {ECO:0000269|PubMed:23515315}.
CC   -!- SIMILARITY: Belongs to the Hha/YmoA/Cnu family. {ECO:0000305}.
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DR   EMBL; AE006468; AAL19427.1; -; Genomic_DNA.
DR   RefSeq; NP_459468.1; NC_003197.2.
DR   RefSeq; WP_001280991.1; NC_003197.2.
DR   PDB; 4ICG; X-ray; 2.92 A; C/D=1-72.
DR   PDBsum; 4ICG; -.
DR   AlphaFoldDB; Q7CR17; -.
DR   SMR; Q7CR17; -.
DR   STRING; 99287.STM0473; -.
DR   PaxDb; Q7CR17; -.
DR   EnsemblBacteria; AAL19427; AAL19427; STM0473.
DR   GeneID; 1251993; -.
DR   GeneID; 67416465; -.
DR   KEGG; stm:STM0473; -.
DR   PATRIC; fig|99287.12.peg.505; -.
DR   HOGENOM; CLU_190629_0_0_6; -.
DR   OMA; RRCQSID; -.
DR   PhylomeDB; Q7CR17; -.
DR   BioCyc; SENT99287:STM0473-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   Gene3D; 1.20.1280.40; -; 1.
DR   InterPro; IPR007985; Hemolysn_expr_modulating_HHA.
DR   InterPro; IPR036666; HHA_sf.
DR   Pfam; PF05321; HHA; 1.
DR   SUPFAM; SSF68989; SSF68989; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..72
FT                   /note="Hemolysin expression-modulating protein Hha"
FT                   /id="PRO_0000436898"
FT   MUTAGEN         14..17
FT                   /note="RLRR->ALRA: Still interacts with H-NS, derepresses
FT                   expression of H-NS/Hha coregulated genes but not genes
FT                   regulated solely by H-NS."
FT                   /evidence="ECO:0000269|PubMed:23515315"
FT   MUTAGEN         14
FT                   /note="R->A: Still interacts with H-NS, derepresses
FT                   expression of H-NS/Hha coregulated genes but not genes
FT                   regulated solely by H-NS."
FT                   /evidence="ECO:0000269|PubMed:23515315"
FT   MUTAGEN         17
FT                   /note="R->A: Still interacts with H-NS, derepresses
FT                   expression of H-NS/Hha coregulated genes but not genes
FT                   regulated solely by H-NS."
FT                   /evidence="ECO:0000269|PubMed:23515315"
FT   MUTAGEN         26
FT                   /note="R->A: Still interacts with H-NS, derepresses
FT                   expression of H-NS/Hha coregulated genes but not genes
FT                   regulated solely by H-NS."
FT                   /evidence="ECO:0000269|PubMed:23515315"
FT   MUTAGEN         48
FT                   /note="D->A: No longer interacts with H-NS, derepresses
FT                   expression of H-NS/Hha coregulated genes but not genes
FT                   regulated solely by H-NS."
FT                   /evidence="ECO:0000269|PubMed:23515315"
FT   HELIX           8..16
FT                   /evidence="ECO:0007829|PDB:4ICG"
FT   HELIX           22..34
FT                   /evidence="ECO:0007829|PDB:4ICG"
FT   HELIX           40..55
FT                   /evidence="ECO:0007829|PDB:4ICG"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:4ICG"
SQ   SEQUENCE   72 AA;  8614 MW;  A63654B87CF1A2FA CRC64;
     MSDKPLTKTD YLMRLRRCQT IDTLERVIEK NKYELSDNEL AVFYSAADHR LAELTMNKLY
     DKIPSSVWKF IR
 
 
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