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Database: UniProt
Entry: A0A0C3MTA4_9PROT
LinkDB: A0A0C3MTA4_9PROT
Original site: A0A0C3MTA4_9PROT 
ID   A0A0C3MTA4_9PROT        Unreviewed;       571 AA.
AC   A0A0C3MTA4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   Name=rpsA {ECO:0000313|EMBL:KIO49928.1};
GN   ORFNames=SQ11_03210 {ECO:0000313|EMBL:KIO49928.1};
OS   Nitrosospira sp. NpAV.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=58133 {ECO:0000313|EMBL:KIO49928.1, ECO:0000313|Proteomes:UP000031969};
RN   [1] {ECO:0000313|EMBL:KIO49928.1, ECO:0000313|Proteomes:UP000031969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NpAV {ECO:0000313|EMBL:KIO49928.1,
RC   ECO:0000313|Proteomes:UP000031969};
RA   Rice M.C., Lim C.K., Sayavedra-Soto L.A., Norton J.M., Klotz M.G.;
RT   "Nitrosospira sp. NpAV genome sequencing.";
RL   Submitted (JAN-2015) 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}.
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:KIO49928.1}.
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DR   EMBL; JXQM01000003; KIO49928.1; -; Genomic_DNA.
DR   RefSeq; WP_041512687.1; NZ_JXQM01000003.1.
DR   AlphaFoldDB; A0A0C3MTA4; -.
DR   OrthoDB; 9804077at2; -.
DR   Proteomes; UP000031969; 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; 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   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:KIO49928.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          30..96
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          114..180
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          201..269
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          286..356
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          373..443
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          460..529
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   571 AA;  63013 MW;  0B67C3569978A531 CRC64;
     MTIASPATES PESFAALFEE SLSRQEMRVG EVITAEVVRV DYNIVVVNAG LKSESFIPVE
     EFKNDKGEIE AKPGDFVSVA IEALEDGYGE TRLSRDKAKR LTAWHDLEAA MESGAIVCGL
     VSGKVKGGLT AMINGIRAFL PGSLVDIRPV KDTTPYENKE MEFKVIKLDR KRNNVVVSRR
     AVLEESQGAD RQSLLANLAE GAVVKGVVKN ITDYGAFVDL GGIDGLLHIT DLAWRRVKHP
     SEVINVGDEV TAKVLKFDQE KNRVSLGMKQ LSEDPWVGLS RRYPQHTRLF GKVSNLTDYG
     AFVEIEQGIE GLVHVSEMDW TNKNVYPSKV VQLGDEVEVM ILEIDEERRR ISLGMKQCKV
     NPWDDFAMNH QKGDKVRGQI KSITDFGVFI GLQGGIDGLV HLSDLSWNQP GEEAVRNYKK
     GDEVEAMVLS IDVERERISL GIKQMEGDPF NSFVSVNDKN SIVKGTVKSI DAKGAVIALE
     NDVEGYLRAS EISRDRVEDI RTHLKEGDTV EAMIINVDRK NRGINLSIKA KDMSEESDAM
     QKVTSDSAAN AGTTSLGALL KAKMDVKNTE Q
//
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