ID M3GM28_LEPBO Unreviewed; 560 AA.
AC M3GM28;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN ORFNames=LEP1GSC123_0434 {ECO:0000313|EMBL:EMG02012.1};
OS Leptospira borgpetersenii str. 200701203.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193007 {ECO:0000313|EMBL:EMG02012.1, ECO:0000313|Proteomes:UP000011783};
RN [1] {ECO:0000313|EMBL:EMG02012.1, ECO:0000313|Proteomes:UP000011783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701203 {ECO:0000313|EMBL:EMG02012.1,
RC ECO:0000313|Proteomes:UP000011783};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025604,
CC ECO:0000256|PIRNR:PIRNR002111}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000256|ARBA:ARBA00006767, ECO:0000256|PIRNR:PIRNR002111}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG02012.1}.
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DR EMBL; AKWO02000010; EMG02012.1; -; Genomic_DNA.
DR AlphaFoldDB; M3GM28; -.
DR BioCyc; LBOR1193007:G11KN-546-MONOMER; -.
DR Proteomes; UP000011783; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 6.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000110; Ribosomal_bS1.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR PANTHER; PTHR10724:SF7; 30S RIBOSOMAL PROTEIN S1, CHLOROPLASTIC; 1.
DR Pfam; PF00575; S1; 5.
DR PIRSF; PIRSF002111; RpsA; 3.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 6.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 6.
DR PROSITE; PS50126; S1; 6.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000011783};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:EMG02012.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 30..92
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 110..176
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 197..265
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 282..352
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 369..439
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 456..525
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 560 AA; 63568 MW; 41C05C089B8BB493 CRC64;
MTNKEEKSTF AEVFKQWEQS IHEEPELRKD QVVEGKIVSV DNDYVYVAIE GLKQEGRIPR
GDFDEAPERG NYVSAIVKRK ESQDSGCVLS KKEADQRKGW EIVKEAFKNG YQVAGRLVNE
IKGKGYIVNV EGVELFLPAS QLSYKFKEGE TFKNKELEFK IIELNDRTRS GVVSRKKLLD
EVNEEKWDAL LLKFKVGDKV KSVVSKIASF GVFCEVDGVT GLLRQRDISY KKYAPFKQYF
QIGQEVELVV LELDKENNKL ALGLKQLYED PWVWAERSLE KEMVIRGTVT SLTKFGAFVE
LKEGLEGLIH TSELAWSKKP PQPKDILKKG QEVEALVLDI DFKNRRLSLG LKQLQPNPWD
QLSPEVRRGN VLEGVITGIT KYGAFVEVEN GIEGLIHISD ITWDEKVSNP TSQLKKGDTV
KYMILDVNLD AQRISCGLKQ LMENPYEIFR NEHPIGTIVE GKVKSIKEFG IFVEVAPGIE
GLVHISEVPN GREVNLAELY KPDETIKTAV IKVDVKNKKI SLSIKDFDKA LEREEMSKYL
KTSDAPSRES LGSFLNTSLR
//
