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Database: UniProt
Entry: M1Z6V9_9FIRM
LinkDB: M1Z6V9_9FIRM
Original site: M1Z6V9_9FIRM 
ID   M1Z6V9_9FIRM            Unreviewed;        88 AA.
AC   M1Z6V9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   28-MAR-2018, entry version 27.
DE   RecName: Full=30S ribosomal protein S17 {ECO:0000256|HAMAP-Rule:MF_01345, ECO:0000256|RuleBase:RU003873};
GN   Name=rpsQ {ECO:0000256|HAMAP-Rule:MF_01345,
GN   ECO:0000313|EMBL:CCQ93741.1};
GN   ORFNames=CULT_150027 {ECO:0000313|EMBL:CCQ93741.1};
OS   [Clostridium] ultunense Esp.
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Tissierellaceae.
OX   NCBI_TaxID=1288971 {ECO:0000313|EMBL:CCQ93741.1, ECO:0000313|Proteomes:UP000011752};
RN   [1] {ECO:0000313|EMBL:CCQ93741.1, ECO:0000313|Proteomes:UP000011752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Esp {ECO:0000313|EMBL:CCQ93741.1,
RC   ECO:0000313|Proteomes:UP000011752};
RX   PubMed=23538905; DOI=10.1128/genomeA.00107-13;
RA   Manzoor S., Muller B., Niazi A., Bongcam-Rudloff E., Schnurer A.;
RT   "Draft Genome Sequence of Clostridium ultunense Strain Esp, a
RT   Syntrophic Acetate-Oxidizing Bacterium.";
RL   Genome Announc. 1:e0010713-e0010713(2013).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC       specifically to the 5'-end of 16S ribosomal RNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01345}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01345}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS17
CC       family. {ECO:0000256|HAMAP-Rule:MF_01345,
CC       ECO:0000256|RuleBase:RU003872, ECO:0000256|SAAS:SAAS00806419}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCQ93741.1}.
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DR   EMBL; CARA01000057; CCQ93741.1; -; Genomic_DNA.
DR   EnsemblBacteria; CCQ93741; CCQ93741; CULT_150027.
DR   OrthoDB; POG091H01FV; -.
DR   Proteomes; UP000011752; Unassembled WGS sequence.
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_01345_B; Ribosomal_S17_B; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019984; Ribosomal_S17.
DR   InterPro; IPR000266; Ribosomal_S17/S11.
DR   InterPro; IPR019979; Ribosomal_S17_CS.
DR   PANTHER; PTHR10744; PTHR10744; 1.
DR   Pfam; PF00366; Ribosomal_S17; 1.
DR   PRINTS; PR00973; RIBOSOMALS17.
DR   ProDom; PD001295; Ribosomal_S17; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR03635; uS17_bact; 1.
DR   PROSITE; PS00056; RIBOSOMAL_S17; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000011752};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011752};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01345,
KW   ECO:0000256|RuleBase:RU003872, ECO:0000256|SAAS:SAAS00023569};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01345,
KW   ECO:0000256|RuleBase:RU003872, ECO:0000256|SAAS:SAAS00023570,
KW   ECO:0000313|EMBL:CCQ93741.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01345,
KW   ECO:0000256|RuleBase:RU003873, ECO:0000256|SAAS:SAAS00673972};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01345,
KW   ECO:0000256|RuleBase:RU003873, ECO:0000256|SAAS:SAAS00673968}.
SQ   SEQUENCE   88 AA;  10318 MW;  8D79716886AF4241 CRC64;
     MAEGRKLRRT FVGKVVSDKM DKTIVVLVET HKRHPLYGKR VKYSKKFKAH DERNEAKIGD
     TVMIMETRPL SRDKHFRLVK IVEKAVIV
//
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