HPF_STAA8
ID HPF_STAA8 Reviewed; 190 AA.
AC Q2G055;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Ribosome hibernation promotion factor {ECO:0000255|HAMAP-Rule:MF_00839};
DE Short=HPF {ECO:0000255|HAMAP-Rule:MF_00839};
DE AltName: Full=Hibernation promoting factor SaHPF {ECO:0000303|PubMed:20015224};
GN Name=hpf {ECO:0000255|HAMAP-Rule:MF_00839, ECO:0000303|PubMed:20015224};
GN OrderedLocusNames=SAOUHSC_00767;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=NBRC 3060;
RX PubMed=20015224; DOI=10.1111/j.1365-2443.2009.01364.x;
RA Ueta M., Wada C., Wada A.;
RT "Formation of 100S ribosomes in Staphylococcus aureus by the hibernation
RT promoting factor homolog SaHPF.";
RL Genes Cells 15:43-58(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
CC -!- FUNCTION: Required for dimerization of active 70S ribosomes into 100S
CC ribosomes; when added to monomeric 70S ribosomes stimulates formation
CC of 100S dimeric ribosomes. Unlike E.coli, 100S ribosomes are present
CC during exponential growth, peak during early stationary phase and then
CC decrease (shown for strain NBRC 3060). {ECO:0000255|HAMAP-
CC Rule:MF_00839, ECO:0000269|PubMed:20015224}.
CC -!- SUBUNIT: Interacts with 100S ribosomes during exponential growth, as
CC 100S ribosomes decrease (after 7 hours) also found associated with 70S
CC ribosomes. {ECO:0000269|PubMed:20015224}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00839,
CC ECO:0000305|PubMed:20015224}.
CC -!- INDUCTION: Expressed by 2 hours growth, increases to maximal
CC concentration by 7 hours and remains high (stationary phase) (at
CC protein level). More protein is found in cells growing under nutrient-
CC deficient conditions. {ECO:0000269|PubMed:20015224}.
CC -!- SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family.
CC Long HPF subfamily. {ECO:0000255|HAMAP-Rule:MF_00839,
CC ECO:0000305|PubMed:20015224}.
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DR EMBL; AB523729; BAI67826.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29898.1; -; Genomic_DNA.
DR RefSeq; WP_000617735.1; NZ_LS483365.1.
DR RefSeq; YP_499325.1; NC_007795.1.
DR PDB; 5ND8; EM; 3.70 A; v=1-190.
DR PDB; 5ND9; EM; 3.70 A; v=1-190.
DR PDB; 5NKO; NMR; -; A/B=131-190.
DR PDB; 6QBZ; NMR; -; A=1-110.
DR PDB; 6T7O; X-ray; 1.60 A; A/B=131-190.
DR PDBsum; 5ND8; -.
DR PDBsum; 5ND9; -.
DR PDBsum; 5NKO; -.
DR PDBsum; 6QBZ; -.
DR PDBsum; 6T7O; -.
DR AlphaFoldDB; Q2G055; -.
DR BMRB; Q2G055; -.
DR SMR; Q2G055; -.
DR STRING; 1280.SAXN108_0819; -.
DR EnsemblBacteria; ABD29898; ABD29898; SAOUHSC_00767.
DR GeneID; 3919059; -.
DR KEGG; sao:SAOUHSC_00767; -.
DR PATRIC; fig|93061.5.peg.692; -.
DR eggNOG; COG1544; Bacteria.
DR HOGENOM; CLU_071472_0_3_9; -.
DR OMA; HGGYGVI; -.
DR PRO; PR:Q2G055; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0045900; P:negative regulation of translational elongation; IBA:GO_Central.
DR GO; GO:0044238; P:primary metabolic process; IEA:InterPro.
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 3D-structure; Cytoplasm; Reference proteome; Translation regulation.
FT CHAIN 1..190
FT /note="Ribosome hibernation promotion factor"
FT /id="PRO_0000291319"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6QBZ"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:6QBZ"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:6QBZ"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6QBZ"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:6QBZ"
FT HELIX 74..98
FT /evidence="ECO:0007829|PDB:6QBZ"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6QBZ"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:6T7O"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:6T7O"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:6T7O"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:6T7O"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:6T7O"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:5NKO"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:6T7O"
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
