ID H5WVF6_9BURK Unreviewed; 274 AA.
AC H5WVF6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000256|HAMAP-Rule:MF_01320};
GN ORFNames=BurJ1DRAFT_0370 {ECO:0000313|EMBL:EHR69262.1};
OS Burkholderiales bacterium JOSHI_001.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR69262.1, ECO:0000313|Proteomes:UP000004674};
RN [1] {ECO:0000313|EMBL:EHR69262.1, ECO:0000313|Proteomes:UP000004674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR69262.1,
RC ECO:0000313|Proteomes:UP000004674};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Lu M., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Smith J., Lewis G.,
RA Woyke T.;
RT "Noncontiguous Finished sequence of Burkholderiales bacterium JOSHI_001.";
RL Submitted (NOV-2011) 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}.
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DR EMBL; CM001438; EHR69262.1; -; Genomic_DNA.
DR AlphaFoldDB; H5WVF6; -.
DR STRING; 864051.BurJ1DRAFT_0370; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_4; -.
DR OrthoDB; 9778722at2; -.
DR BioCyc; BBAC864051:G1H30-366-MONOMER; -.
DR Proteomes; UP000004674; 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:UP000004674};
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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01320};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01320}.
FT DOMAIN 124..252
FT /note="Large ribosomal subunit protein uL2 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01382"
FT REGION 27..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 274 AA; 30196 MW; 33C56BF1CDC38F53 CRC64;
MAVVKVKPTS PGRRAVVKVV HKHLHKGAPE ASLLEPQKQN AGRNNNGHIT MRHKGGGHKH
HYRVVDFKRN KDGIAAKVER IEYDPNRTAH IALVVYADGE RRYIIAPRGL EVGAKLMSGS
EAPIKAGNTL PIRNIPVGST IHCVEMMPGK GAQIARSAGT SVTLMAREGI YSQIRLRSGE
VRKIHIDCRA TIGEVSNEEH NLRQYGKAGA IRWKGIRPTV RGVAMNPVDH PHGGGEGRTG
EGQPQVSPWN TLTKGYRTRN NKRTQTMIVS RRKK
//
