RS5_SYNS9
ID RS5_SYNS9 Reviewed; 215 AA.
AC Q3AW77;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307};
GN Synonyms=rps5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN OrderedLocusNames=Syncc9902_1971;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC -!- FUNCTION: Located at the back of the 30S subunit body where it
CC stabilizes the conformation of the head with respect to the body.
CC {ECO:0000255|HAMAP-Rule:MF_01307}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and
CC S8. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC subunit; the C-terminal domain interacts with the body and contacts
CC protein S4. The interaction surface between S4 and S5 is involved in
CC control of translational fidelity.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000255|HAMAP-Rule:MF_01307}.
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DR EMBL; CP000097; ABB26929.1; -; Genomic_DNA.
DR RefSeq; WP_011360725.1; NC_007513.1.
DR AlphaFoldDB; Q3AW77; -.
DR SMR; Q3AW77; -.
DR STRING; 316279.Syncc9902_1971; -.
DR EnsemblBacteria; ABB26929; ABB26929; Syncc9902_1971.
DR KEGG; sye:Syncc9902_1971; -.
DR eggNOG; COG0098; Bacteria.
DR HOGENOM; CLU_065898_2_1_3; -.
DR OMA; KRGCGSW; -.
DR OrthoDB; 1505038at2; -.
DR Proteomes; UP000002712; 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 Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005712; Ribosomal_S5_bac-type.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..215
FT /note="30S ribosomal protein S5"
FT /id="PRO_1000086070"
FT DOMAIN 59..122
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 215 AA; 22406 MW; 6E9CC2FBCAE754CE CRC64;
MTDSSPQSNP NAVPGAADVP AAAQGQQQEQ RRGGGGGGRG DRRGDRRGGR RGQDRDSEWQ
ERVVQIRRVS KTVKGGKKMS FRAIVVVGNE KGQVGVGVGK AGDVIGAVRK GVADGKKHLV
KVPLTRHSSI PTLSNGRDGA ASVLIRPAAP GTGVIAGGSI RTVLELAGIK NVLAKRLGSK
TPLNNARAAM VALSSLRTHK ETAKERGISL EQIYS
