ID A6T1G1_JANMA Unreviewed; 571 AA.
AC A6T1G1;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN Name=rpsA {ECO:0000313|EMBL:ABR89184.1};
GN OrderedLocusNames=mma_2668 {ECO:0000313|EMBL:ABR89184.1};
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR89184.1, ECO:0000313|Proteomes:UP000006388};
RN [1] {ECO:0000313|EMBL:ABR89184.1, ECO:0000313|Proteomes:UP000006388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille {ECO:0000313|EMBL:ABR89184.1,
RC ECO:0000313|Proteomes:UP000006388};
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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|PIRNR:PIRNR002111}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000256|ARBA:ARBA00006767, ECO:0000256|PIRNR:PIRNR002111}.
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DR EMBL; CP000269; ABR89184.1; -; Genomic_DNA.
DR AlphaFoldDB; A6T1G1; -.
DR STRING; 375286.mma_2668; -.
DR KEGG; mms:mma_2668; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_2_1_4; -.
DR Proteomes; UP000006388; Chromosome.
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; cd05687; S1_RPS1_repeat_ec1_hs1; 1.
DR CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR CDD; cd05688; S1_RPS1_repeat_ec3; 1.
DR CDD; cd05689; S1_RPS1_repeat_ec4; 1.
DR CDD; cd05691; S1_RPS1_repeat_ec6; 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 NCBIfam; TIGR00717; rpsA; 1.
DR PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR PANTHER; PTHR10724:SF13; 30S RIBOSOMAL PROTEIN S1; 1.
DR Pfam; PF00575; S1; 6.
DR PIRSF; PIRSF002111; RpsA; 1.
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:UP000006388};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:ABR89184.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 33..99
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 117..183
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 204..272
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 289..359
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 376..446
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 463..532
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 571 AA; 62534 MW; EF0A2C2F7556FFF5 CRC64;
MTTVVTSEAT PVGMESFAAL FEESLSRQDM RSGEVISAEV VRLDHNFVIV NAGLKSEAFI
PIEEFKNDNG ELEVNVGDFI SVAIESLENG FGDTILSRDK AKRLASWLSL EKAMESGEIV
VGTVNGKVKG GLTVLTNGIR AFLPGSLVDT RPVKDTTPFE GKTLEFKVIK LDRKRNNVVL
SRRAVIEASM GEERQKLMET LKEGTIVTGV VKNITDYGAF VDLGGIDGLL HITDLAWRRV
RHPSEVLTVG QEITAKVLKY DQEKNRVSLG VKQLGDDPWT GLSRRYPQGT RLFGKVTNLT
DYGSFVEVEQ GIEGLVHVSE MDWTNKNVAP NKVVQLGDEV EVMVLEIDEE RRRISLGMKQ
CKANPWDDFA VTHKKGDKVR GAIKSITDFG VFIGLAGNID GLVHLSDLSW TETGEEAVRR
FKKGDELEAI VLAIDVERER VSLGVKQLEG DPFNNFAAMN DKGALVTGTV KSVEPKGAVI
QLSDEVEGYL RASEISRDRV EDAGTHLKVG DTVEAMVINV DRKARGIQLS IKAKDNVETQ
EAMQKMSSDS NAASGTTSLG ALLKAKLDNK N
//
