ID A0A1F4QEQ2_9BACT Unreviewed; 175 AA.
AC A0A1F4QEQ2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Ribosome hibernation promoting factor {ECO:0000256|HAMAP-Rule:MF_00839};
DE Short=HPF {ECO:0000256|HAMAP-Rule:MF_00839};
GN Name=hpf {ECO:0000256|HAMAP-Rule:MF_00839};
GN ORFNames=A3H39_02560 {ECO:0000313|EMBL:OGB93662.1};
OS candidate division NC10 bacterium RIFCSPLOWO2_02_FULL_66_22.
OC Bacteria; candidate division NC10.
OX NCBI_TaxID=1801658 {ECO:0000313|EMBL:OGB93662.1, ECO:0000313|Proteomes:UP000177374};
RN [1] {ECO:0000313|EMBL:OGB93662.1, ECO:0000313|Proteomes:UP000177374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:0000256|HAMAP-Rule:MF_00839}.
CC -!- SUBUNIT: Interacts with 100S ribosomes. {ECO:0000256|HAMAP-
CC Rule:MF_00839}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00839}.
CC -!- SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family.
CC Long HPF subfamily. {ECO:0000256|HAMAP-Rule:MF_00839}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGB93662.1}.
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DR EMBL; METH01000076; OGB93662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4QEQ2; -.
DR STRING; 1801658.A3H39_02560; -.
DR Proteomes; UP000177374; Unassembled WGS sequence.
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; Ribosome hibernation promotion factor-like; 1.
DR Gene3D; 3.30.505.50; Sigma 54 modulation/S30EA ribosomal protein, C-terminal domain; 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 NCBIfam; TIGR00741; yfiA; 1.
DR PANTHER; PTHR33231; 30S RIBOSOMAL PROTEIN; 1.
DR PANTHER; PTHR33231:SF1; 30S RIBOSOMAL PROTEIN; 1.
DR Pfam; PF16321; Ribosom_S30AE_C; 1.
DR Pfam; PF02482; Ribosomal_S30AE; 1.
DR SUPFAM; SSF69754; Ribosome binding protein Y (YfiA homologue); 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00839};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW Rule:MF_00839}.
FT DOMAIN 114..170
FT /note="Sigma 54 modulation/S30EA ribosomal protein C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16321"
SQ SEQUENCE 175 AA; 19838 MW; DA97C08134C615F6 CRC64;
MQFSVTGRNL DITPALRGYA EEKLNRLTRY LEDIVAIHVV LSVAKHRQIA EVTLRVRDLT
IRAEEESDDM YSSLDLVAEK LERQILRYKG RIVAHATRGT NRGGRVAAVA PVVEEEPPVV
KTKRFAIKPA GVDEAILQMN LLGHSFYVFR NALTEEVNVV YRRRDGHYGL IEPEA
//
