ID A0A2A5W0K4_9BACT Unreviewed; 548 AA.
AC A0A2A5W0K4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN Name=rpsA {ECO:0000313|EMBL:PDH30035.1};
GN ORFNames=CNC89_01630 {ECO:0000313|EMBL:PDH30035.1};
OS Puniceicoccaceae bacterium MED-G31.
OC Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales; Puniceicoccaceae.
OX NCBI_TaxID=1986245 {ECO:0000313|EMBL:PDH30035.1, ECO:0000313|Proteomes:UP000219700};
RN [1] {ECO:0000313|EMBL:PDH30035.1, ECO:0000313|Proteomes:UP000219700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G31 {ECO:0000313|EMBL:PDH30035.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-2017) 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:PDH30035.1}.
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DR EMBL; NTJW01000006; PDH30035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5W0K4; -.
DR Proteomes; UP000219700; 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 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; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:PDH30035.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 16..79
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 97..162
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 183..251
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 268..338
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 355..425
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 442..511
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 548 AA; 61448 MW; 48F437B4C39C25B8 CRC64;
MEELLKGSNV ENLNEGSIIK GTIIEIRPTE VVVDIGGKSE GIVHANEFVD ISELQVGSEI
EVYLEKLEDR EGNPIVSYDK AEQKKNWEKI VENCEEGSII PGRVRSKVKG GLIVSIGVDS
FLPASQIDVQ PPKNLDQYVG QTYDFKVVKI NLDRKNIVVS RRELIEEQRM EKRRSLLEQV
KPGDKRRGQV KNITDYGAFV DLDGLDGLLH ITDMSWGRIQ HPSEMVKQGE EIEVIIIEID
RERERVSLGL KQLADNPWEK IEERYPVGAT VSGKVVNLVP YGAFIEIEEG VEGLVHVTEL
SWTKRITKPG EVLRIGEEIQ AVVLGIQKEE QKISLGTRQL DANPWDMARH NYPVGARVRG
KIRNLTTYGA FVELEEGIDG MVHVSDMSWT RKVNHPSEVV KKGDEVDATV LDVDADSQRI
SLGMKQLSSD PWDEIETHYK IGDVVKGKAS KITNYGAFIE LDNDIDGLVH ISQISEERIE
AIKDVIDEGA EVKARVIKID KDERRIGLSI KAANYSDEDL AKERQAFDNV SAVEDLTNLG
DLLDEATK
//
