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 27-MAR-2024, entry version 89. DE RecName: Full=Small ribosomal subunit protein bS1 {ECO:0000305}; DE AltName: Full=30S ribosomal protein S1; GN Name=rpsA; OrderedLocusNames=RT0508; OS Rickettsia typhi (strain ATCC VR-144 / Wilmington). OC Bacteria; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017197; AAU03978.1; -; Genomic_DNA. DR RefSeq; WP_011190959.1; NC_006142.1. DR AlphaFoldDB; Q68WL4; -. DR KEGG; rty:RT0508; -. DR eggNOG; COG0539; Bacteria. DR HOGENOM; CLU_015805_2_1_5; -. DR OrthoDB; 9804077at2; -. DR Proteomes; UP000000604; 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 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; Ribonucleoprotein; Ribosomal protein; RNA-binding. FT CHAIN 1..568 FT /note="Small ribosomal subunit protein bS1" 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 //