RS1_LEULA
ID RS1_LEULA Reviewed; 429 AA.
AC P50889; P71450;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=30S ribosomal protein S1;
GN Name=rps1;
OS Leuconostoc lactis.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=1246;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9034319; DOI=10.1016/s0378-1119(96)00636-1;
RA Yamit-Hezi A., Levy Z., Neuman S., Nudel U.;
RT "A Leuconostoc lactis protein with homology to ribosomal protein S1 shares
RT common epitopes and common DNA binding properties with a mammalian DNA
RT binding nuclear factor.";
RL Gene 185:99-103(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-429.
RX PubMed=7721096; DOI=10.1016/0378-1119(94)00898-3;
RA Eklund E.A., Lee S.W., Skalnik D.G.;
RT "Cloning of a cDNA encoding a human DNA-binding protein similar to
RT ribosomal protein S1.";
RL Gene 155:231-235(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-429.
RX PubMed=8568274;
RA Tsuzaka K., Leu A.K., Frank M.B., Movafagh B.F., Koscec M., Winkler T.H.,
RA Kalden J.R., Reichlin M.;
RT "Lupus autoantibodies to double-stranded DNA cross-react with ribosomal
RT protein S1.";
RL J. Immunol. 156:1668-1675(1996).
CC -!- FUNCTION: Binds mRNA; thus facilitating recognition of the initiation
CC point. It is needed to translate mRNA with a short Shine-Dalgarno (SD)
CC purine-rich sequence (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:7721096 and PubMed:8568274) thought to
CC originate from human but is most probably the result of a cDNA library
CC contamination by L.lactis. {ECO:0000305}.
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DR EMBL; U24086; AAB08978.1; -; Genomic_DNA.
DR EMBL; U05589; AAA77669.1; -; mRNA.
DR EMBL; U27517; AAA97575.1; -; mRNA.
DR AlphaFoldDB; P50889; -.
DR STRING; 1246.JMEA01000003_gene977; -.
DR eggNOG; COG0539; Bacteria.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR10724:SF7; PTHR10724:SF7; 2.
DR Pfam; PF00575; S1; 4.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 4.
DR SUPFAM; SSF50249; SSF50249; 4.
DR PROSITE; PS50126; S1; 4.
PE 2: Evidence at transcript level;
KW Repeat; Ribonucleoprotein; Ribosomal protein; RNA-binding.
FT CHAIN 1..429
FT /note="30S ribosomal protein S1"
FT /id="PRO_0000196040"
FT DOMAIN 55..128
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 144..211
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 231..299
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 316..385
FT /note="S1 motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 382..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 24
FT /note="S -> G (in Ref. 2; AAA77669)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="A -> S (in Ref. 3; AAA97575)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="L -> R (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 46386 MW; 92AC82605F39DDFC CRC64;
MAHALKRILY ATWYPDILVN YTHSVNCRRT LDVMSETNNE FLAALESAAD QIKVGDVVTG
ELLAIDNDNQ AVVGLSTGEE GVVPAREYSD DRNINLADEL KIGDTIEAVV ISNVTSDKEG
VAYLLSKKRL DARKAWENLS FAEGDTVDAK VINAVRGGLI VDVNGVRGFV PASMVAERFV
SDLNQFKNKD IKAQVIEIDP ANARLILSRK AVAAQELAAQ LAEVFSKLSV GEVVEGTVAR
LTDFGAFVDL GGVDGLVHVS EISHDRVKNP ADVLTKGDKV DVKILALDTE KGRISLSIKA
TQRGPWDEAA DQIAAGSVLE GTVKRVKDFG AFVEILPGIE GLVHVSQISN KRIENPSEVL
KSGDKVQVKV LDIKPAEERI SLSMKALEEK PEREDRRGND GSASRADIAA YKQQDDSAAT
LGDIFGDKL