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Database: UniProt
Entry: A0A0K8J9V0_9FIRM
LinkDB: A0A0K8J9V0_9FIRM
Original site: A0A0K8J9V0_9FIRM 
ID   A0A0K8J9V0_9FIRM        Unreviewed;       179 AA.
AC   A0A0K8J9V0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=P22_0473 {ECO:0000313|EMBL:CUH94407.1};
OS   Propionispora sp. 2/2-37.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Propionispora.
OX   NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH94407.1, ECO:0000313|Proteomes:UP000041641};
RN   [1] {ECO:0000313|EMBL:CUH94407.1, ECO:0000313|Proteomes:UP000041641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2/2 {ECO:0000313|EMBL:CUH94407.1};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CYSP01000002; CUH94407.1; -; Genomic_DNA.
DR   RefSeq; WP_054258610.1; NZ_CYSP01000002.1.
DR   AlphaFoldDB; A0A0K8J9V0; -.
DR   STRING; 1677858.P22_0473; -.
DR   OrthoDB; 9794975at2; -.
DR   Proteomes; UP000041641; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00839};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041641};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW   Rule:MF_00839}.
FT   DOMAIN          122..174
FT                   /note="Sigma 54 modulation/S30EA ribosomal protein C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16321"
FT   COILED          71..98
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   179 AA;  20290 MW;  E834D0EB0D34C820 CRC64;
     MAIHVRGKNI EITPALKDYV AKRVGKVTKY FEALGDITVI LTVEKGRHIV EVTVPINGML
     LRGEEATADM YASIDLVIEK LEKQIEKYKT KLARKMRAGV FKGEFAAAAQ TDEAAMDKED
     LGVVKTKRFA VKPMDVEEAI MQMNLINHDF YVFSNSDTEE VNVIYRRKDG RYGLIEPEF
//
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