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Database: UniProt
Entry: T0VU16_LACLC
LinkDB: T0VU16_LACLC
Original site: T0VU16_LACLC 
ID   T0VU16_LACLC            Unreviewed;       132 AA.
AC   T0VU16;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Small ribosomal subunit protein uS8 {ECO:0000256|ARBA:ARBA00035258, ECO:0000256|HAMAP-Rule:MF_01302};
GN   Name=rpsH {ECO:0000256|HAMAP-Rule:MF_01302};
GN   ORFNames=LLT7_08925 {ECO:0000313|EMBL:EQC83313.1};
OS   Lactococcus cremoris subsp. cremoris TIFN7.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=1234877 {ECO:0000313|EMBL:EQC83313.1, ECO:0000313|Proteomes:UP000015724};
RN   [1] {ECO:0000313|EMBL:EQC83313.1, ECO:0000313|Proteomes:UP000015724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIFN7 {ECO:0000313|EMBL:EQC83313.1,
RC   ECO:0000313|Proteomes:UP000015724};
RX   PubMed=23823494; DOI=10.1038/ismej.2013.108;
RA   Erkus O., de Jager V.C., Spus M., van Alen-Boerrigter I.J.,
RA   van Rijswijck I.M., Hazelwood L., Janssen P.W., van Hijum S.A.,
RA   Kleerebezem M., Smid E.J.;
RT   "Multifactorial diversity sustains microbial community stability.";
RL   ISME J. 7:2126-2136(2013).
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:0000256|HAMAP-Rule:MF_01302}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S5 and
CC       S12. {ECO:0000256|HAMAP-Rule:MF_01302}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS8 family.
CC       {ECO:0000256|ARBA:ARBA00006471, ECO:0000256|HAMAP-Rule:MF_01302,
CC       ECO:0000256|RuleBase:RU003660}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQC83313.1}.
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DR   EMBL; ATBA01000297; EQC83313.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0VU16; -.
DR   SMR; T0VU16; -.
DR   PATRIC; fig|1234877.3.peg.2658; -.
DR   Proteomes; UP000015724; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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   Gene3D; 3.30.1370.30; -; 1.
DR   Gene3D; 3.30.1490.10; -; 1.
DR   HAMAP; MF_01302_B; Ribosomal_S8_B; 1.
DR   InterPro; IPR000630; Ribosomal_uS8.
DR   InterPro; IPR047863; Ribosomal_uS8_CS.
DR   InterPro; IPR035987; Ribosomal_uS8_sf.
DR   PANTHER; PTHR11758:SF4; 37S RIBOSOMAL PROTEIN S8, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11758; 40S RIBOSOMAL PROTEIN S15A; 1.
DR   Pfam; PF00410; Ribosomal_S8; 1.
DR   SUPFAM; SSF56047; Ribosomal protein S8; 1.
DR   PROSITE; PS00053; RIBOSOMAL_S8; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01302};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01302};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01302};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01302}.
SQ   SEQUENCE   132 AA;  14670 MW;  7C96AF3B7C61F517 CRC64;
     MVMTDPIADF LTRIRNGNMR KFDVVEAPAS KIKRQIAEIL KAEGYVKDVE YVEDNKQGVI
     RVFLKYGKNG EKVITNLKRI SKPGLRVYVK SDDVPKVLNG LGTAIISTST GVVTDKVARQ
     TNVGGEVIAY IW
//
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