HPF_STACT
ID HPF_STACT Reviewed; 188 AA.
AC P47995; B9DJM1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ribosome hibernation promotion factor {ECO:0000255|HAMAP-Rule:MF_00839};
DE Short=HPF {ECO:0000255|HAMAP-Rule:MF_00839};
GN Name=hpf {ECO:0000255|HAMAP-Rule:MF_00839}; OrderedLocusNames=Sca_0400;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-188.
RX PubMed=7557338; DOI=10.1016/0378-1097(95)00267-9;
RA Klein M., Meens J., Freudl R.;
RT "Functional characterization of the Staphylococcus carnosus SecA protein in
RT Escherichia coli and Bacillus subtilis secA mutant strains.";
RL FEMS Microbiol. Lett. 131:271-277(1995).
CC -!- FUNCTION: Required for dimerization of active 70S ribosomes into 100S
CC ribosomes in stationary phase; 100S ribosomes are translationally
CC inactive and sometimes present during exponential growth.
CC {ECO:0000255|HAMAP-Rule:MF_00839}.
CC -!- SUBUNIT: Interacts with 100S ribosomes. {ECO:0000255|HAMAP-
CC Rule:MF_00839}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00839}.
CC -!- SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family.
CC Long HPF subfamily. {ECO:0000255|HAMAP-Rule:MF_00839}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56161.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AM295250; CAL27314.1; -; Genomic_DNA.
DR EMBL; X79725; CAA56161.1; ALT_FRAME; Genomic_DNA.
DR PIR; S47148; S47148.
DR RefSeq; WP_015899659.1; NC_012121.1.
DR AlphaFoldDB; P47995; -.
DR SMR; P47995; -.
DR STRING; 396513.SCA_0400; -.
DR PRIDE; P47995; -.
DR GeneID; 60545903; -.
DR KEGG; sca:SCA_0400; -.
DR eggNOG; COG1544; Bacteria.
DR HOGENOM; CLU_071472_0_3_9; -.
DR OMA; HGGYGVI; -.
DR OrthoDB; 1766263at2; -.
DR BioCyc; SCAR396513:SCA_RS02040-MON; -.
DR Proteomes; UP000000444; 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 3: Inferred from homology;
KW Cytoplasm; Translation regulation.
FT CHAIN 1..188
FT /note="Ribosome hibernation promotion factor"
FT /id="PRO_0000208591"
FT REGION 93..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 52
FT /note="Missing (in Ref. 2; CAA56161)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="L -> I (in Ref. 2; CAA56161)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="L -> K (in Ref. 2; CAA56161)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="R -> C (in Ref. 2; CAA56161)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="H -> T (in Ref. 2; CAA56161)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="N -> KLICDI (in Ref. 2; CAA56161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21886 MW; 25E12963AB332A5F CRC64;
MIRFEIHGDN LTITDAIRNY IEDKVGKLER YFTNVPNVNA HVKVKTYANS STKIEVTIPL
NDVTLRAEER NDDLYAGIDL ITNKLERQVR KYKTRVNRKK RKESEHEPFP ATPETPPETA
VDHDKDDEIE IIRSKQFSLK PMDSEEAVLQ MDLLGHDFFI FNDRETDGTS IVYRRKDGKY
GLIETVEN