ID A0A268TH31_9HELI Unreviewed; 160 AA.
AC A0A268TH31;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Large ribosomal subunit protein uL10 {ECO:0000256|ARBA:ARBA00035202, ECO:0000256|HAMAP-Rule:MF_00362};
GN Name=rplJ {ECO:0000256|HAMAP-Rule:MF_00362};
GN ORFNames=BKH45_00110 {ECO:0000313|EMBL:PAF43716.1};
OS Helicobacter sp. 11S03491-1.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1476196 {ECO:0000313|EMBL:PAF43716.1, ECO:0000313|Proteomes:UP000216568};
RN [1] {ECO:0000313|EMBL:PAF43716.1, ECO:0000313|Proteomes:UP000216568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11S03491-1 {ECO:0000313|EMBL:PAF43716.1,
RC ECO:0000313|Proteomes:UP000216568};
RX PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT independent niche adaptation followed by diversification in a
RT poikilothermic host.";
RL Sci. Rep. 7:8387-8387(2017).
CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central role in
CC the interaction of the ribosome with GTP-bound translation factors.
CC {ECO:0000256|HAMAP-Rule:MF_00362}.
CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. The
CC N-terminus interacts with L11 and the large rRNA to form the base of
CC the stalk. The C-terminus forms an elongated spine to which L12 dimers
CC bind in a sequential fashion forming a multimeric L10(L12)X complex.
CC {ECO:0000256|HAMAP-Rule:MF_00362}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000256|ARBA:ARBA00008889, ECO:0000256|HAMAP-Rule:MF_00362}.
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:PAF43716.1}.
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DR EMBL; MLAO01000001; PAF43716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268TH31; -.
DR OrthoDB; 3186107at2; -.
DR Proteomes; UP000216568; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd05797; Ribosomal_L10; 1.
DR Gene3D; 3.30.70.1730; -; 1.
DR HAMAP; MF_00362; Ribosomal_L10; 1.
DR InterPro; IPR001790; Ribosomal_uL10.
DR InterPro; IPR043141; Ribosomal_uL10-like_sf.
DR InterPro; IPR022973; Ribosomal_uL10_bac.
DR InterPro; IPR047865; Ribosomal_uL10_bac_type.
DR PANTHER; PTHR11560; 39S RIBOSOMAL PROTEIN L10, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11560:SF8; 39S RIBOSOMAL PROTEIN L10, MITOCHONDRIAL; 1.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR SUPFAM; SSF160369; Ribosomal protein L10-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000216568};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00362};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00362}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00362};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00362}.
SQ SEQUENCE 160 AA; 17971 MW; A885A7A2CF3BD28B CRC64;
MTKHQKEQAV EYLSSEFKSA SALLVCDYKG LAVKNLEELR KSAGNSEIKV QVIKNTLAKI
SMNNAGYPDL DLKDTNIFIW GQDQITLSKL AAKFAEANKE KFVIKTGCFD NKKVETDHIM
AISKLPGRDE LIGMLLSVWT APARYFVTGL DNLKKQKEQE
//