ID A0A0E3U421_9ENTR Unreviewed; 562 AA.
AC A0A0E3U421;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN Name=rpsA {ECO:0000313|EMBL:AKC59946.1};
GN ORFNames=BTURN675_371 {ECO:0000313|EMBL:AKC59946.1};
OS Blochmannia endosymbiont of Polyrhachis (Hedomyrma) turneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=1505596 {ECO:0000313|EMBL:AKC59946.1, ECO:0000313|Proteomes:UP000033094};
RN [1] {ECO:0000313|EMBL:AKC59946.1, ECO:0000313|Proteomes:UP000033094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=675 {ECO:0000313|EMBL:AKC59946.1,
RC ECO:0000313|Proteomes:UP000033094};
RX PubMed=25861561;
RA Williams L.E., Wernegreen J.J.;
RT "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene loss
RT among Blochmannia spanning the origin of the ant tribe Camponotini.";
RL PeerJ 3:E881-E881(2015).
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; CP010048; AKC59946.1; -; Genomic_DNA.
DR RefSeq; WP_046288852.1; NZ_CP010048.1.
DR AlphaFoldDB; A0A0E3U421; -.
DR STRING; 1505596.BTURN675_371; -.
DR KEGG; bed:BTURN675_371; -.
DR PATRIC; fig|1505596.4.peg.376; -.
DR HOGENOM; CLU_015805_2_1_6; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000033094; 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 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; 5.
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:UP000033094};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:AKC59946.1}; 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..516
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 562 AA; 63169 MW; BF3CFF75A5BDBF8C CRC64;
MTESFIQLLE ESFKRIKTSP GSIIRGTIIS IQNDIVLVDA GLKSESPIPI EQFYNSQGVL
EIKVGDQVDV TLDAVEDGFG ETILSREKAK RYESWLILEK AYEEVSTVVG IINGRVKGGF
TVELNGIKAF LPGSLVDIRP IRENMNLEGK EFEFKVIKLD QKRNNVVVSR RAVLESENIS
ERNQLLEQLH EGMQIKGIVK NLTDYGAFID LGGVDGLLHI TDIAWKRIRH PSEVVGIGDE
IIVKVLKFDR EKNRVSLGLK QLEEDPWTAI TKRYHEGMRL TGKVTNLTDY GCFVEMEGGI
EGLVHISEMD WTSKNIHPSK VVNVGEFIEV MLLDIDESRR RISLGLKQCT VNPWEQFLET
YNKGDSVIGK IKSITDFGIF IGLEGGIDGL VHLSDISWHL SIEEIMQKYK KGDEVAAVIL
QVDAERERIS LSIKHLEEDP LNIYLSLNQK KKVVTGTILS INTKGMSVKL TDMIVGYVLF
SDVDKQNEKT YNIGDNIEVK CNGIDRKSRM INLSIPFVIN DFDNTNSKII NSPNASKQSK
DVKQNFSNVM TEAFKAATKT DS
//
