ID M1N275_BARAA Unreviewed; 566 AA.
AC M1N275;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN Name=rpsA {ECO:0000313|EMBL:AGF73989.1};
GN OrderedLocusNames=BAnh1_00960 {ECO:0000313|EMBL:AGF73989.1};
OS Bartonella australis (strain Aust/NH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=1094489 {ECO:0000313|EMBL:AGF73989.1, ECO:0000313|Proteomes:UP000011729};
RN [1] {ECO:0000313|EMBL:AGF73989.1, ECO:0000313|Proteomes:UP000011729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aust/NH1 {ECO:0000313|EMBL:AGF73989.1,
RC ECO:0000313|Proteomes:UP000011729};
RX PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL PLoS Genet. 9:E1003393-E1003393(2013).
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; CP003123; AGF73989.1; -; Genomic_DNA.
DR RefSeq; WP_015397498.1; NC_020300.1.
DR AlphaFoldDB; M1N275; -.
DR STRING; 1094489.BAnh1_00960; -.
DR KEGG; baus:BAnh1_00960; -.
DR PATRIC; fig|1094489.3.peg.117; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_2_1_5; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000011729; 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; cd05691; S1_RPS1_repeat_ec6; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 5.
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:AGF73989.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 27..93
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 111..177
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 198..266
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 283..353
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 370..440
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 459..529
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 566 AA; 63021 MW; 5B9E138B77FF7DF7 CRC64;
MSQYNPTTAD FETLLMESFQ VNDLNEGSVV KGRIIAIEKD MAIVDAGLKV EGRIPLKEFG
TKGKDGSLQV GDEVEVYIER IENAMGEAVL SREKARREES WLRLEEKFNA GVRVDGVIFS
QVKGGFTVDL DGAVAFLPRS QVDIRPIRDV APLMHNPQSF EILKMDRRRG NIVVSRRTVL
EESRAEQRSE IVQNLEESQI VEGVVKNITD YGAFIDLGGI DGLLHVTDMA WRRVNHPSEI
LTIGQTIKVQ IIRINQDTHR ISLGMKQLES DPWDSISLKY PIGKKITGAV TNITDYGGFV
EIEPGIEGLI HVSEMSWTKK NIHPGKLLST SQEVEVVVLE VDPSKRRISL GLKQTFENPW
VAFVNKFPVN SQVEGEVKNK TEFGLFIGLE GDVDGMVHLS DLDWNRPGEQ VIDTYNKGDI
VKAVVLDVDV EKERISLGIK QLSGDKVGEA AAHGELRKGA IVTCEVTGIN DNCIDVKLID
HDLETTIRRN DLARDRDEQR PERFSIGQRV DARIIAFDKK TRKLSVSIKA LEIAEEKEAV
AQYGSMDSGA SLGDILGAAL KKQEQD
//
