UniProtKB - Q2FIN9 (HPF_STAA3)
Protein
Ribosome hibernation promotion factor
Gene
hpf
Organism
Staphylococcus aureus (strain USA300)
Status
Functioni
Required and sufficient for dimerization of active 70S ribosomes into 100S ribosomes. 110S ribosomes are probably translationally inactive and may serve as a reservoir of easily reactivated ribosomes when necessary in the cell. Also reduces the translation efficiency of a small number of genes. Unlike E.coli, 100S ribosomes are present during exponential growth and decrease during stationary phase. This strain produces 30% fewer 100S ribosomes than strain N315 and RN4200 under the same growth conditions (PubMed:27001516).UniRule annotation1 Publication
GO - Biological processi
- primary metabolic process Source: InterPro
- regulation of translation Source: UniProtKB-UniRule
Keywordsi
Biological process | Translation regulation |
Names & Taxonomyi
Protein namesi | Recommended name: Ribosome hibernation promotion factorUniRule annotationShort name: HPF1 PublicationUniRule annotation Alternative name(s): Ribosome hibernation-promoting factor1 Publication |
Gene namesi | Name:hpf1 PublicationUniRule annotation Ordered Locus Names:SAUSA300_0736 |
Organismi | Staphylococcus aureus (strain USA300) |
Taxonomic identifieri | 367830 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation1 Publication
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
400-fold decreased cell survival in long-term growth, effects are more pronounced in minimal medium. No visible formation of 100S ribosomes, rapid degradation of ribosomes once cells have reached stationary phase.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 27 – 30 | KLER → ALEA: Decreased dimerization of 70S ribosomes to 100S ribosomes, still binds 70S ribosomes. Loss of ribosome binding; when associated with 84-A--A-87. 1 Publication | 4 | |
Mutagenesisi | 51 | A → C: No change in 70S ribosome dimerization. 1 Publication | 1 | |
Mutagenesisi | 71 | N → C: No change in 70S ribosome dimerization. 1 Publication | 1 | |
Mutagenesisi | 84 – 87 | KLER → ALEA: Very little dimerization of 70S ribosomes to 100S ribosomes, still binds 70S ribosomes. Loss of ribosome binding; when associated with 27-A--A-30. 1 Publication | 4 | |
Mutagenesisi | 113 | L → C: No change in 70S ribosome dimerization. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000291320 | 1 – 190 | Ribosome hibernation promotion factorAdd BLAST | 190 |
Proteomic databases
PRIDEi | Q2FIN9 |
Interactioni
Subunit structurei
Interacts with 100S ribosomes during exponential growth, as 100S ribosomes decrease (after 28 hours) also found associated with 30s and 50S subunits.
1 PublicationFamily & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 101 – 190 | Required for ribosome-binding1 PublicationAdd BLAST | 90 |
Domaini
The C-terminus (residues 101-190) are required for ribosome-binding; deletion of the last 42 residues partially decreases ribosome-binding.1 Publication
Sequence similaritiesi
Phylogenomic databases
HOGENOMi | CLU_071472_0_3_9 |
OMAi | HGGYGVI |
Family and domain databases
CDDi | cd00552, RaiA, 1 hit |
Gene3Di | 3.30.160.100, 1 hit 3.30.505.50, 1 hit |
HAMAPi | MF_00839, HPF, 1 hit |
InterProi | View protein in InterPro IPR034694, HPF_long/plastid IPR036567, RHF-like IPR003489, RHF/RaiA IPR032528, Ribosom_S30AE_C IPR038416, Ribosom_S30AE_C_sf |
Pfami | View protein in Pfam PF16321, Ribosom_S30AE_C, 1 hit PF02482, Ribosomal_S30AE, 1 hit |
SUPFAMi | SSF69754, SSF69754, 1 hit |
TIGRFAMsi | TIGR00741, yfiA, 1 hit |
i Sequence
Sequence statusi: Complete.
Q2FIN9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MIRFEIHGDN LTITDAIRNY IEEKIGKLER YFNDVPNAVA HVKVKTYSNS
60 70 80 90 100
ATKIEVTIPL KNVTLRAEER NDDLYAGIDL INNKLERQVR KYKTRINRKS
110 120 130 140 150
RDRGDQEVFV AELQEMQETQ VDNDAYDDNE IEIIRSKEFS LKPMDSEEAV
160 170 180 190
LQMNLLGHDF FVFTDRETDG TSIVYRRKDG KYGLIQTSEQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000255 Genomic DNA Translation: ABD20521.1 |
RefSeqi | WP_000617735.1, NZ_CP027476.1 |
Genome annotation databases
EnsemblBacteriai | ABD20521; ABD20521; SAUSA300_0736 |
GeneIDi | 59699391 |
KEGGi | saa:SAUSA300_0736 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000255 Genomic DNA Translation: ABD20521.1 |
RefSeqi | WP_000617735.1, NZ_CP027476.1 |
3D structure databases
SMRi | Q2FIN9 |
ModBasei | Search... |
Proteomic databases
PRIDEi | Q2FIN9 |
Genome annotation databases
EnsemblBacteriai | ABD20521; ABD20521; SAUSA300_0736 |
GeneIDi | 59699391 |
KEGGi | saa:SAUSA300_0736 |
Phylogenomic databases
HOGENOMi | CLU_071472_0_3_9 |
OMAi | HGGYGVI |
Family and domain databases
CDDi | cd00552, RaiA, 1 hit |
Gene3Di | 3.30.160.100, 1 hit 3.30.505.50, 1 hit |
HAMAPi | MF_00839, HPF, 1 hit |
InterProi | View protein in InterPro IPR034694, HPF_long/plastid IPR036567, RHF-like IPR003489, RHF/RaiA IPR032528, Ribosom_S30AE_C IPR038416, Ribosom_S30AE_C_sf |
Pfami | View protein in Pfam PF16321, Ribosom_S30AE_C, 1 hit PF02482, Ribosomal_S30AE, 1 hit |
SUPFAMi | SSF69754, SSF69754, 1 hit |
TIGRFAMsi | TIGR00741, yfiA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HPF_STAA3 | |
Accessioni | Q2FIN9Primary (citable) accession number: Q2FIN9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 12, 2007 |
Last sequence update: | March 21, 2006 | |
Last modified: | April 7, 2021 | |
This is version 72 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |