RS1_RICTY
ID RS1_RICTY Reviewed; 568 AA.
AC Q68WL4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=30S ribosomal protein S1;
GN Name=rpsA; OrderedLocusNames=RT0508;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000305}.
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DR EMBL; AE017197; AAU03978.1; -; Genomic_DNA.
DR RefSeq; WP_011190959.1; NC_006142.1.
DR AlphaFoldDB; Q68WL4; -.
DR STRING; 257363.RT0508; -.
DR EnsemblBacteria; AAU03978; AAU03978; RT0508.
DR KEGG; rty:RT0508; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_2_1_5; -.
DR OMA; SLNEFRY; -.
DR OrthoDB; 1235756at2; -.
DR Proteomes; UP000000604; Chromosome.
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 Gene3D; 2.40.50.140; -; 6.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR000110; Ribosomal_S1.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR10724:SF7; PTHR10724:SF7; 2.
DR Pfam; PF00575; S1; 6.
DR PIRSF; PIRSF002111; RpsA; 1.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 6.
DR SUPFAM; SSF50249; SSF50249; 6.
DR TIGRFAMs; TIGR00717; rpsA; 1.
DR PROSITE; PS50126; S1; 6.
PE 3: Inferred from homology;
KW Repeat; Ribonucleoprotein; Ribosomal protein; RNA-binding.
FT CHAIN 1..568
FT /note="30S ribosomal protein S1"
FT /id="PRO_0000286648"
FT DOMAIN 39..100
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 118..184
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 205..273
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 290..360
FT /note="S1 motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 377..447
FT /note="S1 motif 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 464..533
FT /note="S1 motif 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
SQ SEQUENCE 568 AA; 63875 MW; FE0C7BF001DEB7E2 CRC64;
MSIKLKQRFV PQLAAINYQF EEDFSKMLKT VDTSHIKEKT VVKGQVIEIK NDMIIVDVGL
KNEGRIPKSE FLSLPEVGDV VEVFIEKIEG RNGRTILSRE KAVKEELWGQ LEIMCSKGEF
VDGTIFGRVK GGFTVDLSGV VAFLPGSQVD VRPIKDPTSI MNIKQPFKIL SMDKKLGNIV
VSRRVILEES RSEARDEMLS KIKEGMILEG VVKNITDYGA FIDLGSVDGL LHLTDISWGR
VNHPSEVLEF NQKVKVMVIK FDEKTKRISL GIKQLDSNPW DAIKEEFPVG KKMTGKVTNF
ADYGVFLELK DGLEGLVHSS EISWLKSNQN PRKMLTIGQE VEFIVLEVDT EKHRVSLSIK
QCQENPLIKF AENNPIGTII KAPIRNITDF GIFVVLGNNM DGMIHEGDIS WEDNGTDLLK
SYKKGDEIEC KVLAINFEKE QVSLGIKQLS PNPYQKISDE YKKGTIVKAV VTEIKDDGLV
VLLNNKVTGF IKRVELSDEK DEQKPEMFQV DEEIDAKVVS IEKSTGRVLL SVKAHKIAER
QKTLKEYGSS DNTTNMGDIL ANVLEEKK