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Database: UniProt
Entry: A0A1C3L4E7_9ENTR
LinkDB: A0A1C3L4E7_9ENTR
Original site: A0A1C3L4E7_9ENTR 
ID   A0A1C3L4E7_9ENTR        Unreviewed;       206 AA.
AC   A0A1C3L4E7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   08-NOV-2023, entry version 30.
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:SBT82089.1};
GN   ORFNames=TRABTM_A_02510 {ECO:0000313|EMBL:SBT82089.1};
OS   secondary endosymbiont of Trabutina mannipara.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=1835721 {ECO:0000313|EMBL:SBT82089.1, ECO:0000313|Proteomes:UP000092809};
RN   [1] {ECO:0000313|Proteomes:UP000092809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Szabo Gitta;
RL   Submitted (JUN-2016) 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; LT594522; SBT82089.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C3L4E7; -.
DR   STRING; 1835721.TRABTM_A_02510; -.
DR   KEGG; senm:TRABTM_A_02510; -.
DR   PATRIC; fig|1835721.3.peg.233; -.
DR   OrthoDB; 9803672at2; -.
DR   Proteomes; UP000092809; Chromosome i.
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:UP000092809};
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..95
FT                   /note="Small ribosomal subunit protein uS4 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01390"
FT   DOMAIN          96..160
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
SQ   SEQUENCE   206 AA;  23950 MW;  5294522D0E7BFF31 CRC64;
     MARYLGPKLK LSRRENTDLF LKSGVQAINS KCKIEQIPGQ HGTRKIRLSD YGIQLREKQK
     VRRIYGVLER QFHNYYKEAV RRKGNTGENL LQLLESRLDN VVYRIGFGAT RAESRQLVSH
     KAIIVNGRIV NIASYQVTKN DVISINEKAK KQSRIMASLE LSNQREKPTW IEINFDKMEG
     IFKKYPERTD LSADINEHLI VELYSK
//
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