UniProt: A0A086XW73

Database: UniProt
Entry: A0A086XW73_9RHOB

LinkDB:  A0A086XW73_9RHOB 
Original site:  A0A086XW73_9RHOB

All links

Ontology (5)   
   GO (5)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (14)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
   SMART (2)   
All databases (23)   

Download RDF

ID   A0A086XW73_9RHOB        Unreviewed;       278 AA.
AC   A0A086XW73;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000256|HAMAP-Rule:MF_01320,
GN   ECO:0000313|EMBL:KFI26273.1};
GN   ORFNames=CN97_03855 {ECO:0000313|EMBL:KFI26273.1}, HmaOT1_10770
GN   {ECO:0000313|EMBL:QBJ24691.1};
OS   Haematobacter massiliensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Haematobacter.
OX   NCBI_TaxID=195105 {ECO:0000313|EMBL:KFI26273.1, ECO:0000313|Proteomes:UP000028826};
RN   [1] {ECO:0000313|EMBL:KFI26273.1, ECO:0000313|Proteomes:UP000028826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 47968 {ECO:0000313|EMBL:KFI26273.1,
RC   ECO:0000313|Proteomes:UP000028826};
RA   Wang D., Wang G.;
RT   "Genome of Haematobacter massiliensis CCUG 47968.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QBJ24691.1, ECO:0000313|Proteomes:UP000291082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT1 {ECO:0000313|EMBL:QBJ24691.1,
RC   ECO:0000313|Proteomes:UP000291082};
RA   Lee K.;
RT   "The first complete genome sequence of Haematobacter massiliensis OT1
RT   isolated from human skin.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the primary rRNA binding proteins. Required for
CC       association of the 30S and 50S subunits to form the 70S ribosome, for
CC       tRNA binding and peptide bond formation. It has been suggested to have
CC       peptidyltransferase activity; this is somewhat controversial. Makes
CC       several contacts with the 16S rRNA in the 70S ribosome.
CC       {ECO:0000256|HAMAP-Rule:MF_01320}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC       subunit in the 70S ribosome. {ECO:0000256|HAMAP-Rule:MF_01320}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000256|ARBA:ARBA00005636, ECO:0000256|HAMAP-Rule:MF_01320}.
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; JGYG01000018; KFI26273.1; -; Genomic_DNA.
DR   EMBL; CP035510; QBJ24691.1; -; Genomic_DNA.
DR   RefSeq; WP_035714292.1; NZ_NIPY01000023.1.
DR   AlphaFoldDB; A0A086XW73; -.
DR   STRING; 195105.CN97_03855; -.
DR   KEGG; hml:HmaOT1_10770; -.
DR   eggNOG; COG0090; Bacteria.
DR   OrthoDB; 9778722at2; -.
DR   Proteomes; UP000028826; Unassembled WGS sequence.
DR   Proteomes; UP000291082; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 4.10.950.10; Ribosomal protein L2, domain 3; 1.
DR   HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR002171; Ribosomal_uL2.
DR   InterPro; IPR005880; Ribosomal_uL2_bac/org-type.
DR   InterPro; IPR022669; Ribosomal_uL2_C.
DR   InterPro; IPR022671; Ribosomal_uL2_CS.
DR   InterPro; IPR014726; Ribosomal_uL2_dom3.
DR   InterPro; IPR022666; Ribosomal_uL2_RNA-bd_dom.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   NCBIfam; TIGR01171; rplB_bact; 1.
DR   PANTHER; PTHR13691:SF5; 39S RIBOSOMAL PROTEIN L2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13691; RIBOSOMAL PROTEIN L2; 1.
DR   Pfam; PF00181; Ribosomal_L2; 1.
DR   Pfam; PF03947; Ribosomal_L2_C; 1.
DR   PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR   SMART; SM01383; Ribosomal_L2; 1.
DR   SMART; SM01382; Ribosomal_L2_C; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR   PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000028826};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01320};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01320};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01320};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01320}.
FT   DOMAIN          124..252
FT                   /note="Large ribosomal subunit protein uL2 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01382"
FT   REGION          225..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   278 AA;  30144 MW;  BA9C6AB4510621A8 CRC64;
     MALKSYKPTT PGQRGLVLID RSELWKGRPV KSLTEGLTKN GGRNNTGRIT MRRKGGGAKR
     LYRIVDFKRT KFDVAAVVER IEYDPNRTAF IALVKYEDGE QAYILAPQRL AVGDKVVAGA
     KTDVKPGNAM PFSGMPLGTI VHNVELKPGK GGQIARAAGT YAQFVGRDGG YAQIRLSSGE
     LRMVRQECMA TVGAVSNPDN SNQNLGKAGR NRHLGIRPSV RGVAMNPIDH PHGGGEGRTS
     GGRTPVTPWG KDTKGKKTRS NKATDKYIVR SRHAKKGR
//

DBGET integrated database retrieval system