ID A0A1L8ZBR2_BORBI Unreviewed; 209 AA.
AC A0A1L8ZBR2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000256|ARBA:ARBA00035244, ECO:0000256|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000256|HAMAP-Rule:MF_01328};
GN ORFNames=ER70_04245 {ECO:0000313|EMBL:OJH15172.1};
OS Borrelia bissettiae (Borreliella bissettiae).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=64897 {ECO:0000313|EMBL:OJH15172.1, ECO:0000313|Proteomes:UP000183624};
RN [1] {ECO:0000313|EMBL:OJH15172.1, ECO:0000313|Proteomes:UP000183624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO275 {ECO:0000313|EMBL:OJH15172.1,
RC ECO:0000313|Proteomes:UP000183624};
RX PubMed=26419825; DOI=10.1099/mic.0.000192;
RA Leydet B.F.Jr., Liang F.T.;
RT "Similarities in murine infection and immune response to Borrelia bissettii
RT and Borrelia burgdorferi sensu stricto.";
RL Microbiology 161:2352-2360(2015).
CC -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC {ECO:0000256|HAMAP-Rule:MF_01328}.
CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC initially binds near the 5'-end of the 23S rRNA. It is important during
CC the early stages of 50S assembly. It makes multiple contacts with
CC different domains of the 23S rRNA in the assembled 50S subunit and
CC ribosome. {ECO:0000256|HAMAP-Rule:MF_01328}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01328}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000256|ARBA:ARBA00010528, ECO:0000256|HAMAP-Rule:MF_01328}.
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:OJH15172.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JNBW01000205; OJH15172.1; -; Genomic_DNA.
DR RefSeq; WP_071983471.1; NZ_JNBW01000205.1.
DR AlphaFoldDB; A0A1L8ZBR2; -.
DR OrthoDB; 9803201at2; -.
DR Proteomes; UP000183624; 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: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 Gene3D; 3.40.1370.10; -; 1.
DR HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR InterPro; IPR002136; Ribosomal_uL4.
DR InterPro; IPR013005; Ribosomal_uL4-like.
DR InterPro; IPR023574; Ribosomal_uL4_dom_sf.
DR NCBIfam; TIGR03953; rplD_bact; 1.
DR PANTHER; PTHR10746:SF6; 39S RIBOSOMAL PROTEIN L4, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10746; 50S RIBOSOMAL PROTEIN L4; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; Ribosomal protein L4; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01328};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01328}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01328};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}.
FT REGION 47..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 23478 MW; 5DC3E6F42341CAE1 CRC64;
MEKKVFSKDG KEIGTINLDD RVFNIEISHG SIYNAIKNEL SNLRVGTSST KTRSEVRGSS
KKPWKQKGTG RARVGTKRNP IWIGGGIALG PKPRDYSYRL PKKVKKLAFK SVLSLRAADE
NSFKVIENFN IESGKTKDLA LIIKNFASFN GKVVVLLGND DQMIKRAGKN IRDLKILSFD
KLRVVDLFYA KNLIALESAV NKLNEFYIK
//
