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Database: UniProt
Entry: A0A2P2BVI7_9FIRM
LinkDB: A0A2P2BVI7_9FIRM
Original site: A0A2P2BVI7_9FIRM 
ID   A0A2P2BVI7_9FIRM        Unreviewed;       143 AA.
AC   A0A2P2BVI7;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Large ribosomal subunit protein uL16 {ECO:0000256|HAMAP-Rule:MF_01342};
GN   Name=rplP {ECO:0000256|HAMAP-Rule:MF_01342};
GN   ORFNames=FRIFI_2860 {ECO:0000313|EMBL:CEI74375.1};
OS   Romboutsia hominis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Romboutsia.
OX   NCBI_TaxID=1507512 {ECO:0000313|EMBL:CEI74375.1, ECO:0000313|Proteomes:UP000245695};
RN   [1] {ECO:0000313|EMBL:CEI74375.1, ECO:0000313|Proteomes:UP000245695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRIFI {ECO:0000313|EMBL:CEI74375.1,
RC   ECO:0000313|Proteomes:UP000245695};
RA   Hornung B.V.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds 23S rRNA and is also seen to make contacts with the A
CC       and possibly P site tRNAs. {ECO:0000256|HAMAP-Rule:MF_01342,
CC       ECO:0000256|RuleBase:RU004414}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01342, ECO:0000256|RuleBase:RU004414}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC       {ECO:0000256|ARBA:ARBA00008931, ECO:0000256|HAMAP-Rule:MF_01342,
CC       ECO:0000256|RuleBase:RU004413}.
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DR   EMBL; LN650648; CEI74375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P2BVI7; -.
DR   Proteomes; UP000245695; Chromosome Chromosome1.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd01433; Ribosomal_L16_L10e; 1.
DR   Gene3D; 3.90.1170.10; Ribosomal protein L10e/L16; 1.
DR   HAMAP; MF_01342; Ribosomal_L16; 1.
DR   InterPro; IPR047873; Ribosomal_uL16.
DR   InterPro; IPR000114; Ribosomal_uL16_bact-type.
DR   InterPro; IPR020798; Ribosomal_uL16_CS.
DR   InterPro; IPR016180; Ribosomal_uL16_dom.
DR   InterPro; IPR036920; Ribosomal_uL16_sf.
DR   NCBIfam; TIGR01164; rplP_bact; 1.
DR   PANTHER; PTHR12220:SF13; 39S RIBOSOMAL PROTEIN L16, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12220; 50S/60S RIBOSOMAL PROTEIN L16; 1.
DR   Pfam; PF00252; Ribosomal_L16; 1.
DR   PRINTS; PR00060; RIBOSOMALL16.
DR   SUPFAM; SSF54686; Ribosomal protein L16p/L10e; 1.
DR   PROSITE; PS00586; RIBOSOMAL_L16_1; 1.
DR   PROSITE; PS00701; RIBOSOMAL_L16_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000245695};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01342};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01342};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01342};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01342,
KW   ECO:0000256|RuleBase:RU004414};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01342,
KW   ECO:0000256|RuleBase:RU004414}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   143 AA;  16068 MW;  90D8A5518F9C91C1 CRC64;
     MLMPKRVKRR RVHRGSMAGK AHKGNKVTYG EFGLVALEAS WITSNQIEAA RIAMTRSIKR
     GGKVWIKIFP HKPVTRKPAE TRMGAGKGSP EYWVAVVKPG RVMFELAGVS EEKAREAMRL
     AMHKLPVKCK FVKREDLEVK GGE
//
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