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Database: UniProt
Entry: A0A2X5BZ19_SERRU
LinkDB: A0A2X5BZ19_SERRU
Original site: A0A2X5BZ19_SERRU 
ID   A0A2X5BZ19_SERRU        Unreviewed;       580 AA.
AC   A0A2X5BZ19;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   Name=rpsA {ECO:0000313|EMBL:VEI72198.1};
GN   ORFNames=NCTC10036_04613 {ECO:0000313|EMBL:VEI72198.1}, NCTC9419_04508
GN   {ECO:0000313|EMBL:VEA72891.1};
OS   Serratia rubidaea (Serratia marinorubra).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=61652 {ECO:0000313|EMBL:VEI72198.1, ECO:0000313|Proteomes:UP000281904};
RN   [1] {ECO:0000313|Proteomes:UP000271603, ECO:0000313|Proteomes:UP000281904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10036 {ECO:0000313|EMBL:VEI72198.1,
RC   ECO:0000313|Proteomes:UP000281904}, and NCTC9419
RC   {ECO:0000313|EMBL:VEA72891.1, ECO:0000313|Proteomes:UP000271603};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) 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|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; LR134155; VEA72891.1; -; Genomic_DNA.
DR   EMBL; LR134493; VEI72198.1; -; Genomic_DNA.
DR   STRING; 61652.AXX16_3482; -.
DR   Proteomes; UP000271603; Chromosome 1.
DR   Proteomes; UP000281904; Chromosome 1.
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; cd05690; S1_RPS1_repeat_ec5; 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.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:VEI72198.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111, ECO:0000256|PROSITE-
KW   ProRule:PRU00182}.
FT   DOMAIN          44..110
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          128..194
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          215..283
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          300..370
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          387..457
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          474..543
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   580 AA;  63917 MW;  4006160DF0D9E130 CRC64;
     MLNNPIRRDA KWTLNQRTLK IINMTESFAQ LFEESLKSIE TRPGSIVRGV VVAIDKDVVL
     VDAGLKSESA IPAEQFKNAQ GELEIQVGDE VDVALDAVED GFGETLLSRE KAKRHEAWIT
     LEKAYEDAET VTGVINGKVK GGFTVELNGI RAFLPGSLVD VRPVRDTLHL EGKELEFKVI
     KLDQKRNNVV VSRRAVIESE NSAERDQLLE NLQEGMEVKG IVKNLTDYGA FVDLGGVDGL
     LHITDMAWKR VKHPSEIVNV GDEITVKVLK FDRERTRVSL GLKQLGEDPW VAIAKRYPEG
     TKLTGRVTNL TDYGCFVEIE EGVEGLVHVS EMDWTNKNIH PSKVVNVGDV VEVMVLDIDE
     ERRRISLGLK QCKSNPWQQF AETHNKGDRV EGKIKSITDF GIFIGLDGGI DGLVHLSDIS
     WNVAGEEAVR EYKKGDEIAA VVLQVDAERE RISLGVKQLA EDPFNNYLSM NKKGAIVTGK
     VTAVDAKGAT VELAGGVEGY LRASEASRDR VEDATLVLNV GDDVEAKFTG VDRKNRVVSL
     SVRAKDEADE KDAIATVNNK QEEGNFSNAM AEAFKAAKGE
//
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