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Database: UniProt
Entry: U1GP78_TRESO
LinkDB: U1GP78_TRESO
Original site: U1GP78_TRESO 
ID   U1GP78_TRESO            Unreviewed;       204 AA.
AC   U1GP78;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:ERF59805.1};
GN   ORFNames=HMPREF1325_0932 {ECO:0000313|EMBL:ERF59805.1};
OS   Treponema socranskii subsp. socranskii VPI DR56BR1116 = ATCC 35536.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=1125725 {ECO:0000313|EMBL:ERF59805.1, ECO:0000313|Proteomes:UP000016412};
RN   [1] {ECO:0000313|EMBL:ERF59805.1, ECO:0000313|Proteomes:UP000016412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VPI DR56BR1116 {ECO:0000313|EMBL:ERF59805.1,
RC   ECO:0000313|Proteomes:UP000016412};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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   -!- 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:ERF59805.1}.
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DR   EMBL; AUZJ01000058; ERF59805.1; -; Genomic_DNA.
DR   RefSeq; WP_021331282.1; NZ_AVQI01000022.1.
DR   AlphaFoldDB; U1GP78; -.
DR   STRING; 1125725.HMPREF1325_0932; -.
DR   PATRIC; fig|1125725.3.peg.2254; -.
DR   eggNOG; COG0522; Bacteria.
DR   OrthoDB; 9803672at2; -.
DR   Proteomes; UP000016412; 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; 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; 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          2..94
FT                   /note="Small ribosomal subunit protein uS4 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01390"
FT   DOMAIN          95..155
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          28..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  23209 MW;  CE8BC411F3B10D8E CRC64;
     MAVKQPKGKI VRRLGTNIFG NPKYSKLLTK RPNAPGKERG AKQRGKTSVY GEQLKEKQKF
     RLAYGMSEKQ FRNLFARAQR MEGITSDNML SLMEQRFDNT VFRMGFAVSR AQARQMVSHC
     YFYVNGKPAN IPSMRIKAKD VITSKEKKGI QNLIRHNLVS VQGNRGSWLT VDEEKLSATV
     TSLPSANDIQ PVGNIQYVIE FYSR
//
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