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HPF_STAA3
ID   HPF_STAA3               Reviewed;         190 AA.
AC   Q2FIN9;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Ribosome hibernation promotion factor {ECO:0000255|HAMAP-Rule:MF_00839};
DE            Short=HPF {ECO:0000255|HAMAP-Rule:MF_00839, ECO:0000303|PubMed:27001516};
DE   AltName: Full=Ribosome hibernation-promoting factor {ECO:0000303|PubMed:27001516};
GN   Name=hpf {ECO:0000255|HAMAP-Rule:MF_00839, ECO:0000303|PubMed:27001516};
GN   OrderedLocusNames=SAUSA300_0736;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
RN   [2]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF 27-LYS--ARG-30; ALA-51; ASN-71; 84-LYS--ARG-87 AND LEU-113.
RC   STRAIN=USA300;
RX   PubMed=27001516; DOI=10.1093/nar/gkw180;
RA   Basu A., Yap M.F.;
RT   "Ribosome hibernation factor promotes Staphylococcal survival and
RT   differentially represses translation.";
RL   Nucleic Acids Res. 44:4881-4893(2016).
CC   -!- FUNCTION: Required and sufficient for dimerization of active 70S
CC       ribosomes into 100S ribosomes. 110S ribosomes are probably
CC       translationally inactive and may serve as a reservoir of easily
CC       reactivated ribosomes when necessary in the cell. Also reduces the
CC       translation efficiency of a small number of genes. Unlike E.coli, 100S
CC       ribosomes are present during exponential growth and decrease during
CC       stationary phase. This strain produces 30% fewer 100S ribosomes than
CC       strain N315 and RN4200 under the same growth conditions
CC       (PubMed:27001516). {ECO:0000255|HAMAP-Rule:MF_00839,
CC       ECO:0000269|PubMed:27001516}.
CC   -!- SUBUNIT: Interacts with 100S ribosomes during exponential growth, as
CC       100S ribosomes decrease (after 28 hours) also found associated with 30s
CC       and 50S subunits. {ECO:0000269|PubMed:27001516}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00839,
CC       ECO:0000305|PubMed:27001516}.
CC   -!- DOMAIN: The C-terminus (residues 101-190) is required for ribosome-
CC       binding; deletion of the last 42 residues partially decreases ribosome-
CC       binding. {ECO:0000269|PubMed:27001516}.
CC   -!- DISRUPTION PHENOTYPE: 400-fold decreased cell survival in long-term
CC       growth, effects are more pronounced in minimal medium. No visible
CC       formation of 100S ribosomes, rapid degradation of ribosomes once cells
CC       have reached stationary phase. {ECO:0000269|PubMed:27001516}.
CC   -!- SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family.
CC       Long HPF subfamily. {ECO:0000255|HAMAP-Rule:MF_00839}.
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DR   EMBL; CP000255; ABD20521.1; -; Genomic_DNA.
DR   RefSeq; WP_000617735.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FIN9; -.
DR   SMR; Q2FIN9; -.
DR   PRIDE; Q2FIN9; -.
DR   EnsemblBacteria; ABD20521; ABD20521; SAUSA300_0736.
DR   KEGG; saa:SAUSA300_0736; -.
DR   HOGENOM; CLU_071472_0_3_9; -.
DR   OMA; HGGYGVI; -.
DR   Proteomes; UP000001939; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0044238; P:primary metabolic process; IEA:InterPro.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00552; RaiA; 1.
DR   Gene3D; 3.30.160.100; -; 1.
DR   Gene3D; 3.30.505.50; -; 1.
DR   HAMAP; MF_00839; HPF; 1.
DR   InterPro; IPR034694; HPF_long/plastid.
DR   InterPro; IPR036567; RHF-like.
DR   InterPro; IPR003489; RHF/RaiA.
DR   InterPro; IPR032528; Ribosom_S30AE_C.
DR   InterPro; IPR038416; Ribosom_S30AE_C_sf.
DR   Pfam; PF16321; Ribosom_S30AE_C; 1.
DR   Pfam; PF02482; Ribosomal_S30AE; 1.
DR   SUPFAM; SSF69754; SSF69754; 1.
DR   TIGRFAMs; TIGR00741; yfiA; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Translation regulation.
FT   CHAIN           1..190
FT                   /note="Ribosome hibernation promotion factor"
FT                   /id="PRO_0000291320"
FT   REGION          101..190
FT                   /note="Required for ribosome-binding"
FT                   /evidence="ECO:0000269|PubMed:27001516"
FT   MUTAGEN         27..30
FT                   /note="KLER->ALEA: Decreased dimerization of 70S ribosomes
FT                   to 100S ribosomes, still binds 70S ribosomes. Loss of
FT                   ribosome binding; when associated with 84-A--A-87."
FT                   /evidence="ECO:0000269|PubMed:27001516"
FT   MUTAGEN         51
FT                   /note="A->C: No change in 70S ribosome dimerization."
FT                   /evidence="ECO:0000269|PubMed:27001516"
FT   MUTAGEN         71
FT                   /note="N->C: No change in 70S ribosome dimerization."
FT                   /evidence="ECO:0000269|PubMed:27001516"
FT   MUTAGEN         84..87
FT                   /note="KLER->ALEA: Very little dimerization of 70S
FT                   ribosomes to 100S ribosomes, still binds 70S ribosomes.
FT                   Loss of ribosome binding; when associated with 27-A--A-30."
FT                   /evidence="ECO:0000269|PubMed:27001516"
FT   MUTAGEN         113
FT                   /note="L->C: No change in 70S ribosome dimerization."
FT                   /evidence="ECO:0000269|PubMed:27001516"
SQ   SEQUENCE   190 AA;  22213 MW;  D6987D197B42FE15 CRC64;
     MIRFEIHGDN LTITDAIRNY IEEKIGKLER YFNDVPNAVA HVKVKTYSNS ATKIEVTIPL
     KNVTLRAEER NDDLYAGIDL INNKLERQVR KYKTRINRKS RDRGDQEVFV AELQEMQETQ
     VDNDAYDDNE IEIIRSKEFS LKPMDSEEAV LQMNLLGHDF FVFTDRETDG TSIVYRRKDG
     KYGLIQTSEQ
 
 
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