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IRAP_SALTI
ID   IRAP_SALTI              Reviewed;          86 AA.
AC   Q8XG49; Q7ANH8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Anti-adapter protein IraP {ECO:0000255|HAMAP-Rule:MF_01198};
GN   Name=iraP {ECO:0000255|HAMAP-Rule:MF_01198};
GN   OrderedLocusNames=STY0415, t2481;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
CC   -!- FUNCTION: Inhibits RpoS proteolysis by regulating RssB activity,
CC       thereby increasing the stability of the sigma stress factor RpoS
CC       especially during phosphate and magnesium starvation, but also in
CC       stationary phase and during nitrogen starvation. Its effect on RpoS
CC       stability is due to its interaction with RssB, which probably blocks
CC       the interaction of RssB with RpoS, and the consequent delivery of the
CC       RssB-RpoS complex to the ClpXP protein degradation pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_01198}.
CC   -!- SUBUNIT: Interacts with RssB. {ECO:0000255|HAMAP-Rule:MF_01198}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01198}.
CC   -!- SIMILARITY: Belongs to the IraP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01198}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO70069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAD08838.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014613; AAO70069.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL513382; CAD08838.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_454978.1; NC_003198.1.
DR   RefSeq; WP_001518423.1; NZ_WNTL01000012.1.
DR   AlphaFoldDB; Q8XG49; -.
DR   SMR; Q8XG49; -.
DR   STRING; 220341.16501652; -.
DR   EnsemblBacteria; AAO70069; AAO70069; t2481.
DR   KEGG; stt:t2481; -.
DR   KEGG; sty:STY0415; -.
DR   PATRIC; fig|220341.7.peg.412; -.
DR   eggNOG; ENOG5032SF1; Bacteria.
DR   HOGENOM; CLU_169517_0_0_6; -.
DR   OMA; IDTAMIH; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01198; Anti_adapt_IraP; 1.
DR   InterPro; IPR019732; SigmaS_Anti-adapt_IraP.
DR   Pfam; PF10796; Anti-adapt_IraP; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Stress response.
FT   CHAIN           1..86
FT                   /note="Anti-adapter protein IraP"
FT                   /id="PRO_0000337862"
FT   COILED          1..36
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01198"
SQ   SEQUENCE   86 AA;  9883 MW;  1F904287C95EB24C CRC64;
     MKNLIAELLL KLAQKEEESK ELVAQVEALE IIVTAMLRNM AQNEQEMLIR QVEGALEGVK
     PDASVPDHDT ELLRQYVKKL LRHPRH
 
 
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