ID RS5_SHESM Reviewed; 167 AA.
AC Q0HNS0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Small ribosomal subunit protein uS5 {ECO:0000255|HAMAP-Rule:MF_01307};
DE AltName: Full=30S ribosomal protein S5 {ECO:0000305};
GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307};
GN OrderedLocusNames=Shewmr4_0216;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. MR-4.";
RL Submitted (AUG-2006) 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; CP000446; ABI37297.1; -; Genomic_DNA.
DR RefSeq; WP_007644438.1; NC_008321.1.
DR AlphaFoldDB; Q0HNS0; -.
DR SMR; Q0HNS0; -.
DR GeneID; 75190601; -.
DR KEGG; she:Shewmr4_0216; -.
DR HOGENOM; CLU_065898_2_2_6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 3.30.160.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_01307_B; Ribosomal_uS5_B; 1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR000851; Ribosomal_uS5.
DR InterPro; IPR005712; Ribosomal_uS5_bac-type.
DR InterPro; IPR005324; Ribosomal_uS5_C.
DR InterPro; IPR013810; Ribosomal_uS5_N.
DR InterPro; IPR018192; Ribosomal_uS5_N_CS.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR01021; rpsE_bact; 1.
DR PANTHER; PTHR48277; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR PANTHER; PTHR48277:SF1; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..167
FT /note="Small ribosomal subunit protein uS5"
FT /id="PRO_0000323200"
FT DOMAIN 12..75
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
SQ SEQUENCE 167 AA; 17741 MW; E554F947D06CBBB8 CRC64;
MAKLEAQQKD DLQEKLIAVN RVSKVVKGGR IFSFTALTVV GDGNGKVGYG YGKAREVPAA
IQKAMEKARR NMVTVELNAG TLHHPVKGRH TGSRVYMQPA SQGTGIIAGG AMRAVLEVAG
VHNVLSKAYG STNPINIVRA TVDALVHMKS PSQIAAKRGL NVDEIRG
//
