RS5_SALTY
ID RS5_SALTY Reviewed; 167 AA.
AC P0A7W4; O54299; P02356;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=30S ribosomal protein S5;
GN Name=rpsE; OrderedLocusNames=STM3423;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=LT2;
RX PubMed=9520473; DOI=10.1073/pnas.95.7.3949;
RA Bjoerkman J., Hughes D., Andersson D.I.;
RT "Virulence of antibiotic-resistant Salmonella typhimurium.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3949-3953(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP CHARACTERIZATION OF VARIANTS.
RC STRAIN=LT2;
RX PubMed=9987109; DOI=10.1046/j.1365-2958.1999.01142.x;
RA Bjoerkman J., Samuelsson P., Andersson D.I., Hughes D.;
RT "Novel ribosomal mutations affecting translational accuracy, antibiotic
RT resistance and virulence of Salmonella typhimurium.";
RL Mol. Microbiol. 31:53-58(1999).
RN [4]
RP REVIEW ON TRANSLATIONAL ACCURACY.
RA Kurland C.G., Hughes D., Ehrenberg M.;
RT "Limitations of translational accuracy.";
RL (In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C.,
RL Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M.,
RL Umbarger H.E. (eds.);
RL Escherichia coli and Salmonella: Cellular and molecular biology (2nd ed.),
RL pp.979-1004, American Society for Microbiology Press, Washington D.C.
RL (1996).
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy. Many suppressors of streptomycin-dependent mutants of protein
CC S12 are found in this protein, some but not all of which decrease
CC translational accuracy (ram, ribosomal ambiguity mutations).
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 -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and
CC S8.
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 -!- MISCELLANEOUS: Altered S5 proteins have been identified in a number of
CC mutants. Some mutations in S5 have been shown to increase translational
CC error frequencies.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
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DR EMBL; AJ223237; CAA11205.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22286.1; -; Genomic_DNA.
DR RefSeq; NP_462327.1; NC_003197.2.
DR RefSeq; WP_000940121.1; NC_003197.2.
DR AlphaFoldDB; P0A7W4; -.
DR SMR; P0A7W4; -.
DR STRING; 99287.STM3423; -.
DR PaxDb; P0A7W4; -.
DR EnsemblBacteria; AAL22286; AAL22286; STM3423.
DR GeneID; 1254946; -.
DR GeneID; 67370899; -.
DR KEGG; stm:STM3423; -.
DR PATRIC; fig|99287.12.peg.3620; -.
DR HOGENOM; CLU_065898_2_2_6; -.
DR OMA; KRGCGSW; -.
DR PhylomeDB; P0A7W4; -.
DR BioCyc; SENT99287:STM3423-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Antibiotic resistance; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..167
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131589"
FT DOMAIN 11..74
FT /note="S5 DRBM"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT VARIANT 102
FT /note="G -> D (confers streptomycin independence on
FT streptomycin-dependent S12 mutant P90L)"
FT VARIANT 109
FT /note="G -> S (in strain: JB279; fast-growing suppressor of
FT streptomycin resistant S12 mutant K42N)"
FT VARIANT 112
FT /note="R -> C (confers streptomycin independence on
FT streptomycin-dependent S12 mutant P90L)"
FT CONFLICT 92
FT /note="S -> L (in Ref. 1; CAA11205)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="F -> I (in Ref. 1; CAA11205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 17603 MW; 0B7EA2CB34018CAB CRC64;
MAHIEKQAGE LQEKLIAVNR VSKTVKGGRI FSFTALTVVG DGNGRVGFGY GKAREVPAAI
QKAMEKARRN MINVALNNGT LQHPVKGVHT GSRVFMQPAS EGTGIIAGGA MRAVLEVAGV
HNVLAKAYGS TNPINVVRAT IDGLENMNSP EMVAAKRGKS VEEILGK
