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Database: UniProt
Entry: A0A220W5F6_9SPHN
LinkDB: A0A220W5F6_9SPHN
Original site: A0A220W5F6_9SPHN 
ID   A0A220W5F6_9SPHN        Unreviewed;       204 AA.
AC   A0A220W5F6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ECO:0000313|EMBL:ASK88025.1};
GN   ORFNames=SPHFLASMR4Y_01259 {ECO:0000313|EMBL:ASK88025.1};
OS   Sphingorhabdus sp. SMR4y.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=2584094 {ECO:0000313|EMBL:ASK88025.1, ECO:0000313|Proteomes:UP000198359};
RN   [1] {ECO:0000313|EMBL:ASK88025.1, ECO:0000313|Proteomes:UP000198359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMR4y {ECO:0000313|EMBL:ASK88025.1,
RC   ECO:0000313|Proteomes:UP000198359};
RA   Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA   Clarke A.K.;
RT   "Genome Sequence of Sphingorhabdus flavimaris Strain SMR4y Isolated from a
RT   culture of the Diatom Skeletonema marinoi.";
RL   Submitted (JUL-2017) 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; CP022336; ASK88025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A220W5F6; -.
DR   KEGG; sfla:SPHFLASMR4Y_01259; -.
DR   OrthoDB; 9803672at2; -.
DR   Proteomes; UP000198359; 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:UP000198359};
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..93
FT                   /note="Small ribosomal subunit protein uS4 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01390"
FT   DOMAIN          94..158
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  23231 MW;  EC86B23F4C022AC1 CRC64;
     MTKRTSSKYK LDRRMGENIW GRPKSPVNRR DYGPGQHGQR RKGKLSDFGI QLRAKQKLKG
     YYGDVTEKQF RRAYKEAAAM KGDTSQNLIG LLEQRLDMVV YRAKFAPTIF AARQLVSHGH
     IRVNGVKCNV ASRKVVPGDE IALSDKAKEM LLVIEAQSLA ERDIPEYVNP EGTDKVTYVR
     VPTLDEVPYP VTMEPNLVVE FYSR
//
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