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Database: UniProt
Entry: A0A0U1KKF0_9BACI
LinkDB: A0A0U1KKF0_9BACI
Original site: A0A0U1KKF0_9BACI 
ID   A0A0U1KKF0_9BACI        Unreviewed;       183 AA.
AC   A0A0U1KKF0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, 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=yvyD {ECO:0000313|EMBL:CQR46412.1};
GN   Synonyms=hpf {ECO:0000256|HAMAP-Rule:MF_00839};
GN   ORFNames=BN1058_00672 {ECO:0000313|EMBL:CQR46412.1};
OS   Paraliobacillus sp. PM-2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Paraliobacillus.
OX   NCBI_TaxID=1462524 {ECO:0000313|EMBL:CQR46412.1, ECO:0000313|Proteomes:UP000199066};
RN   [1] {ECO:0000313|EMBL:CQR46412.1, ECO:0000313|Proteomes:UP000199066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM-2 {ECO:0000313|EMBL:CQR46412.1,
RC   ECO:0000313|Proteomes:UP000199066};
RA   Murphy D.;
RL   Submitted (MAR-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; CTEI01000001; CQR46412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1KKF0; -.
DR   STRING; 1462524.BN1058_00672; -.
DR   OrthoDB; 9794975at2; -.
DR   Proteomes; UP000199066; 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:UP000199066};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW   Rule:MF_00839}.
FT   DOMAIN          124..179
FT                   /note="Sigma 54 modulation/S30EA ribosomal protein C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16321"
FT   COILED          73..100
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   183 AA;  21438 MW;  177A5CC18BD1EC7B CRC64;
     MKYNIRGENV EVTGAIKQYI EKKVSKLERY FDTPPTSDVN VNLSVYNEEQ QIEITIPMTN
     LLLRAEEQHA DLYAAIDLVV DKLERQIRKY KTKVNRKARQ QGAPKHIFAE MEKEAIRENE
     EDEDNFEIVR TKRFDLKPMD SEEAILQMDM LGHTFYVFTN AESGDTNVVY RRRDGKYGLI
     EPS
//
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