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Database: UniProt
Entry: I3VU35_THESW
LinkDB: I3VU35_THESW
Original site: I3VU35_THESW 
ID   I3VU35_THESW            Unreviewed;       276 AA.
AC   I3VU35;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000256|HAMAP-Rule:MF_01320};
GN   OrderedLocusNames=Tsac_1014 {ECO:0000313|EMBL:AFK86030.1};
OS   Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK86030.1, ECO:0000313|Proteomes:UP000006178};
RN   [1] {ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA   Brown S.D., Land M.L., Herring C.D.;
RT   "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFK86030.1, ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX   PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA   Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA   Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT   "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT   Thermoanaerobacterium saccharolyticum during the Degradation of
RT   Hemicellulose.";
RL   Appl. Environ. Microbiol. 80:5001-5011(2014).
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; CP003184; AFK86030.1; -; Genomic_DNA.
DR   RefSeq; WP_014757926.1; NC_017992.1.
DR   AlphaFoldDB; I3VU35; -.
DR   STRING; 1094508.Tsac_1014; -.
DR   KEGG; tsh:Tsac_1014; -.
DR   PATRIC; fig|1094508.3.peg.1026; -.
DR   eggNOG; COG0090; Bacteria.
DR   OMA; SCIELRP; -.
DR   Proteomes; UP000006178; 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   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|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01320}.
FT   DOMAIN          124..253
FT                   /note="Large ribosomal subunit protein uL2 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01382"
FT   REGION          224..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..276
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  30272 MW;  3F38CCD7CF940097 CRC64;
     MGIKKYNPTS PGRRQMTVLT FEEITKDKPE KSLTVSLNKT GGRNVYGRIT VRHRGGGHKR
     KYRIIDFKRD KDGVPGKVAS IEYDPNRSAF IALIHYLDGE KRYIIAPYGL KVGDIVESGE
     NVDIKVGNAL PLSHIPVGTF IHNIELVAGK GGQLVRAAGA MAQLIAKEGD YVQVRMPSSE
     VRRIRSNCRA TIGQVSNLDH ENVTIGKAGR SRWLGIRPTV RGSVMNPVDH PHGGGEGKAP
     IGHPGPMTPW GKPALGYKTR KKNKSTNKMI VKSRKA
//
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