ID   RS8_LEPIC               Reviewed;         133 AA.
AC   Q72NH5;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=30S ribosomal protein S8 {ECO:0000255|HAMAP-Rule:MF_01302};
GN   Name=rpsH {ECO:0000255|HAMAP-Rule:MF_01302}; OrderedLocusNames=LIC_12859;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA central domain where it helps coordinate assembly of the
CC       platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01302}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S5 and
CC       S12. {ECO:0000255|HAMAP-Rule:MF_01302}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS8 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01302}.
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DR   EMBL; AE016823; AAS71412.1; -; Genomic_DNA.
DR   RefSeq; WP_000062824.1; NC_005823.1.
DR   AlphaFoldDB; Q72NH5; -.
DR   SMR; Q72NH5; -.
DR   PaxDb; Q72NH5; -.
DR   EnsemblBacteria; AAS71412; AAS71412; LIC_12859.
DR   GeneID; 61142733; -.
DR   KEGG; lic:LIC_12859; -.
DR   HOGENOM; CLU_098428_0_2_12; -.
DR   OMA; FDQGYIL; -.
DR   Proteomes; UP000007037; Chromosome I.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01302_B; Ribosomal_S8_B; 1.
DR   InterPro; IPR000630; Ribosomal_S8.
DR   InterPro; IPR035987; Ribosomal_S8_sf.
DR   PANTHER; PTHR11758; PTHR11758; 1.
DR   Pfam; PF00410; Ribosomal_S8; 1.
DR   SUPFAM; SSF56047; SSF56047; 1.
DR   PROSITE; PS00053; RIBOSOMAL_S8; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..133
FT                   /note="30S ribosomal protein S8"
FT                   /id="PRO_0000126427"
SQ   SEQUENCE   133 AA;  15119 MW;  BA96A33F92A63614 CRC64;
     MSMSDPIGDM LTRIRNAGRA KHETCLVPGS KIKKSILDLM KEEGFIKDYE SVKVNETFED
     YKVFLKYDHT KRPIIRELVR VSTPGRRVYI KSAEIRPYKN NIGTLIVSTS KGIMTGKNAR
     KLKLGGEVIL KMS