ID A0A0X8GZY5_9FIRM Unreviewed; 200 AA.
AC A0A0X8GZY5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=AOC36_05830 {ECO:0000313|EMBL:AMC93516.1};
OS Erysipelothrix larvae.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Erysipelothrix.
OX NCBI_TaxID=1514105 {ECO:0000313|EMBL:AMC93516.1, ECO:0000313|Proteomes:UP000063781};
RN [1] {ECO:0000313|EMBL:AMC93516.1, ECO:0000313|Proteomes:UP000063781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LV19 {ECO:0000313|EMBL:AMC93516.1,
RC ECO:0000313|Proteomes:UP000063781};
RA Lim S., Kim B.-C.;
RT "Erysipelothrix larvae sp. LV19 isolated from the larval gut of the
RT rhinoceros beetle, Trypoxylus dichotomus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP013213; AMC93516.1; -; Genomic_DNA.
DR RefSeq; WP_067632380.1; NZ_CP013213.1.
DR AlphaFoldDB; A0A0X8GZY5; -.
DR STRING; 1514105.AOC36_05830; -.
DR KEGG; erl:AOC36_05830; -.
DR OrthoDB; 9803672at2; -.
DR Proteomes; UP000063781; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000063781};
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 3..91
FT /note="Small ribosomal subunit protein uS4 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01390"
FT DOMAIN 92..156
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
SQ SEQUENCE 200 AA; 23328 MW; 0BD5242F94E94A90 CRC64;
MARIKGPVWK KSRRLSFSVL ETGEELRRRD YAPGQHGKAR RAKLSNYGLQ LREKQRVRFM
YGVSEKQFYN TYLRATKMDG VTGHNFFNLL ESRLDNVVYR MNLARTRRGA RQLVNHGHIL
VDGKKVDIPS YRVTPGQTIE LREKSRNLES VKDALAANVG RVDYVTFDEN TMKGTFTRLP
ERSELNQEIN EALIVEFYNR
//
