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Database: UniProt
Entry: H6N237_GORPV
LinkDB: H6N237_GORPV
Original site: H6N237_GORPV 
ID   H6N237_GORPV            Unreviewed;        93 AA.
AC   H6N237;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Small ribosomal subunit protein bS6 {ECO:0000256|ARBA:ARBA00035294, ECO:0000256|HAMAP-Rule:MF_00360};
GN   Name=rpsF {ECO:0000256|HAMAP-Rule:MF_00360,
GN   ECO:0000313|EMBL:AFA75909.1};
GN   OrderedLocusNames=GPOL_c49150 {ECO:0000313|EMBL:AFA75909.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA75909.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA75909.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA   Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation and
RT   insights into the subsequent degradation pathway revealed by the genome
RT   sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
CC   -!- FUNCTION: Binds together with bS18 to 16S ribosomal RNA.
CC       {ECO:0000256|ARBA:ARBA00035104, ECO:0000256|HAMAP-Rule:MF_00360}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS6 family.
CC       {ECO:0000256|ARBA:ARBA00009512, ECO:0000256|HAMAP-Rule:MF_00360}.
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DR   EMBL; CP003119; AFA75909.1; -; Genomic_DNA.
DR   RefSeq; WP_006373164.1; NC_016906.1.
DR   AlphaFoldDB; H6N237; -.
DR   STRING; 1112204.GPOL_c49150; -.
DR   KEGG; gpo:GPOL_c49150; -.
DR   eggNOG; COG0360; Bacteria.
DR   HOGENOM; CLU_113441_5_3_11; -.
DR   Proteomes; UP000009154; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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   CDD; cd00473; bS6; 1.
DR   Gene3D; 3.30.70.60; -; 1.
DR   HAMAP; MF_00360; Ribosomal_S6; 1.
DR   InterPro; IPR000529; Ribosomal_bS6.
DR   InterPro; IPR020815; Ribosomal_bS6_CS.
DR   InterPro; IPR035980; Ribosomal_bS6_sf.
DR   InterPro; IPR020814; Ribosomal_S6_plastid/chlpt.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribsomal_bS6.
DR   NCBIfam; TIGR00166; S6; 1.
DR   PANTHER; PTHR21011:SF1; 28S RIBOSOMAL PROTEIN S6, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR21011; MITOCHONDRIAL 28S RIBOSOMAL PROTEIN S6; 1.
DR   Pfam; PF01250; Ribosomal_S6; 1.
DR   SUPFAM; SSF54995; Ribosomal protein S6; 1.
DR   PROSITE; PS01048; RIBOSOMAL_S6; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009154};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_00360};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_00360,
KW   ECO:0000313|EMBL:AFA75909.1};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00360};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_00360}.
SQ   SEQUENCE   93 AA;  10677 MW;  0A9D33427C930B47 CRC64;
     MRHYELMVIL DPSLDERTVA PSLDTFLNVV RKDGGKVDNV DIWGKRRLAY EIAKHSEGIY
     AVIDLNAEPN TVSELDRQLK LNESVLRTKV LRK
//
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