ID A0A261FGF0_9BIFI Unreviewed; 208 AA.
AC A0A261FGF0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Small ribosomal subunit protein uS4 {ECO:0000256|ARBA:ARBA00035254, ECO:0000256|HAMAP-Rule:MF_01306};
GN Name=rpsD {ECO:0000256|HAMAP-Rule:MF_01306};
GN ORFNames=BMYO_1759 {ECO:0000313|EMBL:OZG58043.1}, EMO91_10155
GN {ECO:0000313|EMBL:KAA8827120.1};
OS Bifidobacterium myosotis.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1630166 {ECO:0000313|EMBL:OZG58043.1, ECO:0000313|Proteomes:UP000216871};
RN [1] {ECO:0000313|EMBL:OZG58043.1, ECO:0000313|Proteomes:UP000216871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100196 {ECO:0000313|EMBL:OZG58043.1,
RC ECO:0000313|Proteomes:UP000216871};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
RN [2] {ECO:0000313|EMBL:KAA8827120.1, ECO:0000313|Proteomes:UP000410049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RST17 {ECO:0000313|EMBL:KAA8827120.1,
RC ECO:0000313|Proteomes:UP000410049};
RX PubMed=31585749;
RA Modesto M., Satti M., Watanabe K., Puglisi E., Morelli L., Huang C.-H.,
RA Liou J.-S., Miyashita M., Tamura T., Saito S., Mori K., Huang L.,
RA Sciavilla P., Sandri C., Spiezio C., Vitali F., Cavalieri D.,
RA Perpetuini G., Tofalo R., Bonetti A., Arita M., Mattarelli P.;
RT "Characterization of Bifidobacterium species in feaces of the Egyptian
RT fruit bat: Description of B. vespertilionis sp. nov. and B. rousetti sp.
RT nov.";
RL Syst. Appl. Microbiol. 42:126017-126017(2019).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01306}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC interaction surface between S4 and S5 is involved in control of
CC translational fidelity. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000256|ARBA:ARBA00007465, ECO:0000256|HAMAP-Rule:MF_01306,
CC ECO:0000256|RuleBase:RU003699}.
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:OZG58043.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RZUH01000008; KAA8827120.1; -; Genomic_DNA.
DR EMBL; MWWW01000023; OZG58043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261FGF0; -.
DR OrthoDB; 9803672at2; -.
DR Proteomes; UP000216871; Unassembled WGS sequence.
DR Proteomes; UP000410049; Unassembled WGS sequence.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR InterPro; IPR022801; Ribosomal_uS4.
DR InterPro; IPR005709; Ribosomal_uS4_bac-type.
DR InterPro; IPR018079; Ribosomal_uS4_CS.
DR InterPro; IPR001912; Ribosomal_uS4_N.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR NCBIfam; TIGR01017; rpsD_bact; 1.
DR PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1.
DR PANTHER; PTHR11831:SF4; 37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01306};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01306};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01306};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01306}.
FT DOMAIN 5..94
FT /note="Small ribosomal subunit protein uS4 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01390"
FT DOMAIN 95..157
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
SQ SEQUENCE 208 AA; 23740 MW; B38F4D4025A0A7C2 CRC64;
MTNVQRSRRQ VRLSRALGIA LTPKAQRIFE KRPYAPGEHG RTRRRTESDY AVRLREKQRL
RAQYGVSEKQ LRSAYEKGTR VAGQTGNAML IDLETRLDNL VLRSGFARTT AQARQFVVHR
HILVDGNIVD RPSYRVKPGQ TIQVKPKSQT MVPFQIAAEG VHRDVLPAVP GYLDVNLPSL
KATLTRKPEV EQIPVQVNIQ YVVEFYAR
//