RS1_CHLTR
ID RS1_CHLTR Reviewed; 569 AA.
AC O84100;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=30S ribosomal protein S1;
GN Name=rpsA; Synonyms=rs1; OrderedLocusNames=CT_098;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67689.1; -; Genomic_DNA.
DR PIR; A71556; A71556.
DR RefSeq; NP_219601.1; NC_000117.1.
DR RefSeq; WP_009873044.1; NC_000117.1.
DR AlphaFoldDB; O84100; -.
DR STRING; 813.O172_00530; -.
DR EnsemblBacteria; AAC67689; AAC67689; CT_098.
DR GeneID; 884179; -.
DR KEGG; ctr:CT_098; -.
DR PATRIC; fig|272561.5.peg.108; -.
DR HOGENOM; CLU_015805_2_1_0; -.
DR InParanoid; O84100; -.
DR OMA; SLNEFRY; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
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; 3.
DR Pfam; PF00575; S1; 6.
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 Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding.
FT CHAIN 1..569
FT /note="30S ribosomal protein S1"
FT /id="PRO_0000196032"
FT DOMAIN 52..116
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 134..199
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 220..288
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 305..375
FT /note="S1 motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 392..462
FT /note="S1 motif 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 479..548
FT /note="S1 motif 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
SQ SEQUENCE 569 AA; 63574 MW; AB89D73C75902EE1 CRC64;
MPKQADYTWG AKKNLDTIAC LPEDVKQFKD LLYAMYGFTA TEEEPTSEVH PGAILKGTVV
DISKDFVVVD VGLKSEGVIP MSEFIDSSEG LTVGAEVEVY LDQTEDDEGK VVLSREKATR
QRQWEYILAH CEEGSIVKGQ ITRKVKGGLI VDIGMEAFLP GSQIDNKKIK NLDDYVGKVC
EFKILKINVD RRNVVVSRRE LLEAERISKK AELIEQITIG ERRKGIVKNI TDFGVFLDLD
GIDGLLHITD MTWKRIRHPS EMVELNQELE VIILSVDKEK GRVALGLKQK EHNPWEDIEK
KYPPGKRVRG KIVKLLPYGA FIEIEEGIEG LIHVSEMSWV KNIVDPNEVV NKGDEVEVVV
LSIQKDEGKI SLGLKQTKHN PWDNIEEKYP IGLRVTAEIK NLTNYGAFVE LEPGIEGLIH
ISDMSWIKKV SHPSELFKKG NTVEAVILSV DKESKKITLG VKQLTPNPWD EIEVMFPVGS
DISGVVTKIT AFGAFVELQN GIEGLIHVSE LSEKPFAKIE DVLSIGDKVS AKVIKLDPDH
KKVSLSIKEF LVHGGDAGHD AEEESSDRD
