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RL2_CHLTA
ID   RL2_CHLTA               Reviewed;         284 AA.
AC   Q3KLH2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=CTA_0574;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
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:0000255|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:0000255|HAMAP-Rule:MF_01320}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR   EMBL; CP000051; AAX50800.1; -; Genomic_DNA.
DR   RefSeq; WP_009871889.1; NC_007429.1.
DR   AlphaFoldDB; Q3KLH2; -.
DR   SMR; Q3KLH2; -.
DR   EnsemblBacteria; AAX50800; AAX50800; CTA_0574.
DR   KEGG; cta:CTA_0574; -.
DR   HOGENOM; CLU_036235_2_1_0; -.
DR   OMA; SCIELRP; -.
DR   Proteomes; UP000002532; 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; -; 1.
DR   Gene3D; 4.10.950.10; -; 1.
DR   HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR002171; Ribosomal_L2.
DR   InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR   InterPro; IPR022669; Ribosomal_L2_C.
DR   InterPro; IPR022671; Ribosomal_L2_CS.
DR   InterPro; IPR014726; Ribosomal_L2_dom3.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR13691; PTHR13691; 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; SSF50104; SSF50104; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR01171; rplB_bact; 1.
DR   PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..284
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_0000237171"
FT   REGION          28..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..284
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   284 AA;  31473 MW;  8377CA1CF916903C CRC64;
     MFKKFKPVTP GTRQLILPSF DELTTQGELK GSSSRRSVRP NKKLSFFKKS SGGRDNLGHI
     SCRHRGGGVR RHYRVIDFKR NKDGIEAKVA SVEYDPNRSA YIALLNYVDG EKRYILAPKG
     IKRGDRVISG EGSPFKTGCC MTLKSIPLGL SVHNVEMRPG SGGKLVRSAG LSAQIIAKTA
     GYVTLKMPSG EFRMLNEMCR ATVGEVSNAD HNLCVDGKAG RRRWKGIRPT VRGTAMNPVD
     HPHGGGEGRH NGYISQTPWG KVTKGLKTRD KRKSNKWIVK DRRK
 
 
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