ID C0ME65_STRS7 Unreviewed; 400 AA.
AC C0ME65;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Putative 30S ribosomal protein S1 {ECO:0000313|EMBL:CAW99009.1};
GN OrderedLocusNames=SZO_08280 {ECO:0000313|EMBL:CAW99009.1};
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483 {ECO:0000313|Proteomes:UP000001368};
RN [1] {ECO:0000313|EMBL:CAW99009.1, ECO:0000313|Proteomes:UP000001368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70 {ECO:0000313|EMBL:CAW99009.1,
RC ECO:0000313|Proteomes:UP000001368};
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000256|ARBA:ARBA00006767}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM204884; CAW99009.1; -; Genomic_DNA.
DR AlphaFoldDB; C0ME65; -.
DR KEGG; seq:SZO_08280; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_4_5_9; -.
DR Proteomes; UP000001368; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR CDD; cd05692; S1_RPS1_repeat_hs4; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR PANTHER; PTHR10724:SF13; 30S RIBOSOMAL PROTEIN S1; 1.
DR Pfam; PF00575; S1; 4.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 4.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS50126; S1; 4.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000313|EMBL:CAW99009.1};
KW Ribosomal protein {ECO:0000313|EMBL:CAW99009.1}.
FT DOMAIN 17..74
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 107..173
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 194..262
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 279..348
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 351..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 43795 MW; 4EBDAC1F641EA618 CRC64;
MNEFEDLLNS VSEVNPGDVV TAEVLTVDNG QANVVIEGTG VEGVLTLREL TNDREADIND
YVKAGDTVEV LVLRQVVGKD TDTVTFLVSK KRLEARKAWD KLIGREGEVV TVKGTRAVKG
GLSVEFEGLR GFIPASMIDT RFVRNTEKFV GQEFDAKIKE VDAAENRFIL SRREVVEEAA
KQARDKVFST LSEGSVVTGT VARLTSFGAF IDLGGVDGLV HVTELSHERN VSPKSVVSVG
EEVEVKVLAL DEEAGRVSLS LKATTPGPWD GVEQKLAQGD VIEGKVKRLT DFGAFVEVLP
GIDGLVHISQ ISHKRVENPK DVLTVGQEVT VKVLDVNAAD ERVSLSIKAL EERPAQAEGE
KEEKRQSRPR RQKREAKRDY ELPETQTGFS MADLFGDIEL
//
