ID A0A080N2K0_9BIFI Unreviewed; 229 AA.
AC A0A080N2K0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=BBOMB_0549 {ECO:0000313|EMBL:KFF31212.1};
OS Bifidobacterium bombi DSM 19703.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF31212.1, ECO:0000313|Proteomes:UP000028730};
RN [1] {ECO:0000313|EMBL:KFF31212.1, ECO:0000313|Proteomes:UP000028730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF31212.1,
RC ECO:0000313|Proteomes:UP000028730};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(2014).
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:KFF31212.1}.
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DR EMBL; ATLK01000001; KFF31212.1; -; Genomic_DNA.
DR RefSeq; WP_044086723.1; NZ_JDTS01000001.1.
DR AlphaFoldDB; A0A080N2K0; -.
DR STRING; 1341695.BBOMB_0549; -.
DR eggNOG; COG1544; Bacteria.
DR OrthoDB; 9794975at2; -.
DR Proteomes; UP000028730; 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 Reference proteome {ECO:0000313|Proteomes:UP000028730};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW Rule:MF_00839}.
FT DOMAIN 160..214
FT /note="Sigma 54 modulation/S30EA ribosomal protein C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16321"
FT REGION 125..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 25539 MW; 9FA06E08EA1F81A1 CRC64;
MEIVITGRHM EVMQRFRDVA ESKLSRVTSI APDVQRAQIV LTKEGNPRQA DIAKRVEITI
FAGSTVVRAE ASSSDEFSAL DIALDKLTLR LRRTRDKRKD HRRGYNAQVP VDLGVVPVDD
QPVVSQSDEA ARGGVSNSAE EAVSSNLEPG QSVEVKVGDT PIVIRRKLHV AEPMSIDEAL
YEMELIGHDF FLFVNKATGR PSVVYRRHGW SYGVFEIDTP ENIRKSRNG
//
