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Database: UniProt
Entry: A0A1V2QJD3_9PSEU
LinkDB: A0A1V2QJD3_9PSEU
Original site: A0A1V2QJD3_9PSEU 
ID   A0A1V2QJD3_9PSEU        Unreviewed;       146 AA.
AC   A0A1V2QJD3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Small ribosomal subunit protein bS16 {ECO:0000256|HAMAP-Rule:MF_00385};
GN   Name=rpsP {ECO:0000256|HAMAP-Rule:MF_00385};
GN   ORFNames=ALI22I_18325 {ECO:0000313|EMBL:ONI88332.1};
OS   Saccharothrix sp. ALI-22-I.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI88332.1, ECO:0000313|Proteomes:UP000188617};
RN   [1] {ECO:0000313|EMBL:ONI88332.1, ECO:0000313|Proteomes:UP000188617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI88332.1,
RC   ECO:0000313|Proteomes:UP000188617};
RX   PubMed=28087533;
RA   Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA   Kuske C.R.;
RT   "Polysaccharide degradation capability of Actinomycetales soil isolates
RT   from a semi-arid grassland of the Colorado Plateau.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00385}.
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:ONI88332.1}.
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DR   EMBL; MTQP01000059; ONI88332.1; -; Genomic_DNA.
DR   RefSeq; WP_077006745.1; NZ_MTQP01000059.1.
DR   AlphaFoldDB; A0A1V2QJD3; -.
DR   STRING; 1933778.ALI22I_18325; -.
DR   OrthoDB; 9807878at2; -.
DR   Proteomes; UP000188617; Unassembled WGS sequence.
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:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1320.10; -; 1.
DR   HAMAP; MF_00385; Ribosomal_S16; 1.
DR   InterPro; IPR000307; Ribosomal_bS16.
DR   InterPro; IPR023803; Ribosomal_bS16_dom_sf.
DR   NCBIfam; TIGR00002; S16; 1.
DR   PANTHER; PTHR12919; 30S RIBOSOMAL PROTEIN S16; 1.
DR   PANTHER; PTHR12919:SF20; 30S RIBOSOMAL PROTEIN S16, CHLOROPLASTIC; 1.
DR   Pfam; PF00886; Ribosomal_S16; 1.
DR   SUPFAM; SSF54565; Ribosomal protein S16; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000188617};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_00385};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_00385}.
FT   REGION          113..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   146 AA;  15788 MW;  041699130F6D5AF4 CRC64;
     MAVKIKLQRL GKIRQPYYRI VVADARVRRS GKAIETIGKY HPKEEPSFIA VDSDRAQYWL
     GVGAQPTESV QRLLEITGDW QKFKGLPGAE GTLRVKEPKT SKAELFAAAL AAAGDAPSTD
     ATTPKKKSAK KAADAEPAPE AAKDEA
//
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