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Database: UniProt
Entry: A0A0M2LMS4_9MICO
LinkDB: A0A0M2LMS4_9MICO
Original site: A0A0M2LMS4_9MICO 
ID   A0A0M2LMS4_9MICO        Unreviewed;        90 AA.
AC   A0A0M2LMS4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   28-MAR-2018, entry version 15.
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   ORFNames=XM48_12695 {ECO:0000313|EMBL:KKI17034.1};
OS   Leucobacter sp. Ag1.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI17034.1, ECO:0000313|Proteomes:UP000033836};
RN   [1] {ECO:0000313|EMBL:KKI17034.1, ECO:0000313|Proteomes:UP000033836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKI17034.1,
RC   ECO:0000313|Proteomes:UP000033836};
RA   Pei D., Kukutla P., Yu W., Xu J.;
RT   "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT   gambiae.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKI17034.1}.
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DR   EMBL; LAYO01000105; KKI17034.1; -; Genomic_DNA.
DR   RefSeq; WP_046456195.1; NZ_LAYO01000105.1.
DR   EnsemblBacteria; KKI17034; KKI17034; XM48_12695.
DR   PATRIC; fig|1642040.3.peg.2975; -.
DR   Proteomes; UP000033836; 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:UP000033836};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033836};
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:KKI17034.1};
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   90 AA;  10427 MW;  64002231D3D6F4F1 CRC64;
     MAEVEKEQRG YRKARRGYVV SDKMDKTIVV EVEDRVKHPL YGKVLRRSSK VKAHDEQNTA
     GIGDLVLIHE TRPLSASKRW RLVEILEKAK
//
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