ID A0A077F563_9PSED Unreviewed; 558 AA.
AC A0A077F563;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN ORFNames=PSAKL28_13820 {ECO:0000313|EMBL:AIL60608.1};
OS Pseudomonas alkylphenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL60608.1, ECO:0000313|Proteomes:UP000028931};
RN [1] {ECO:0000313|EMBL:AIL60608.1, ECO:0000313|Proteomes:UP000028931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KL28 {ECO:0000313|EMBL:AIL60608.1,
RC ECO:0000313|Proteomes:UP000028931};
RA Lee K., Lim J.Y., Hwang I.;
RL Submitted (JUL-2014) 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}.
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DR EMBL; CP009048; AIL60608.1; -; Genomic_DNA.
DR RefSeq; WP_038608311.1; NZ_CP009048.1.
DR AlphaFoldDB; A0A077F563; -.
DR KEGG; palk:PSAKL28_13820; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_2_1_6; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000028931; 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:SF7; 30S RIBOSOMAL PROTEIN S1, CHLOROPLASTIC; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:AIL60608.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 21..87
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 105..171
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 192..260
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 277..347
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 364..434
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 451..520
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 558 AA; 61588 MW; ECA012FD1C119623 CRC64;
MSESFAELFE ESLKTLNLQP GAIITGIVVD IDGDWVTVHA GLKSEGVIPL EQFYNEAGEL
TIKVGDEVHV ALDAVEDGFG ETKLSREKAK RAECWIVLEA AFAAEEVVKG VINGKVKGGF
TVDVNGIRAF LPGSLVDVRP VRDTTHLEGK ELEFKVIKLD QKRNNVVVSR RSVLEAENSA
EREALLESLQ EGQQVKGIVK NLTDYGAFVD LGGVDGLLHI TDMAWKRIKH PSEIVNVGDE
IDVKVLKYDR ERNRVSLGLK QLGEDPWVAI KARYPESTRV MARVTNLTDY GCFAELEEGV
EGLVHVSEMD WTNKNIHPSK VVQVGDEVEV MVLDIDEERR RISLGIKQCK SNPWEDFSGQ
FNKGDKISGT IKSITDFGIF IGLDGGIDGL VHLSDISWNE VGEEAVRRFK KGDELDTVIL
SVDPERERIS LGIKQLEDDP FSNYVAVNDK GAIVKGIVKE VDAKGAIITL ADDIEATLKA
SEISRDRVED ARNVLKEGEE IEAKIISVDR KSRVISLSIK SKDDAEEKEA IQSLKETAPE
AADTTMAALL RQAMAKQN
//
