ID   RL25_ANAMM              Reviewed;         218 AA.
AC   Q5P9A5;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=50S ribosomal protein L25 {ECO:0000255|HAMAP-Rule:MF_01334};
DE   AltName: Full=General stress protein CTC {ECO:0000255|HAMAP-Rule:MF_01334};
GN   Name=rplY {ECO:0000255|HAMAP-Rule:MF_01334};
GN   Synonyms=ctc {ECO:0000255|HAMAP-Rule:MF_01334}; OrderedLocusNames=AM1340;
OS   Anaplasma marginale (strain St. Maries).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=234826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St. Maries;
RX   PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA   Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA   Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT   "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT   is skewed to two superfamilies of outer membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
CC   -!- FUNCTION: This is one of the proteins that binds to the 5S RNA in the
CC       ribosome where it forms part of the central protuberance.
CC       {ECO:0000255|HAMAP-Rule:MF_01334}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC       rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA
CC       independently of L5 and L18. {ECO:0000255|HAMAP-Rule:MF_01334}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family. CTC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01334}.
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DR   EMBL; CP000030; AAV87125.1; -; Genomic_DNA.
DR   RefSeq; WP_011114690.1; NZ_AFMU01000059.1.
DR   AlphaFoldDB; Q5P9A5; -.
DR   SMR; Q5P9A5; -.
DR   KEGG; ama:AM1340; -.
DR   HOGENOM; CLU_075939_0_1_5; -.
DR   OMA; HVDFYEV; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0008097; F:5S rRNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00495; Ribosomal_L25_TL5_CTC; 1.
DR   Gene3D; 2.170.120.20; -; 1.
DR   Gene3D; 2.40.240.10; -; 1.
DR   HAMAP; MF_01334; Ribosomal_L25_CTC; 1.
DR   InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR   InterPro; IPR029751; Ribosomal_L25.
DR   InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR   InterPro; IPR020057; Ribosomal_L25_b-dom.
DR   InterPro; IPR037121; Ribosomal_L25_C.
DR   InterPro; IPR001021; Ribosomal_L25_long.
DR   Pfam; PF01386; Ribosomal_L25p; 1.
DR   Pfam; PF14693; Ribosomal_TL5_C; 1.
DR   SUPFAM; SSF50715; SSF50715; 1.
DR   TIGRFAMs; TIGR00731; bL25_bact_ctc; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..218
FT                   /note="50S ribosomal protein L25"
FT                   /id="PRO_0000181506"
FT   REGION          187..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   218 AA;  23197 MW;  7EF6A865147E6680 CRC64;
     MSHGDTIRVD ASVRAKCGTG SARALRAAGL IPAVVYGKNR DAVNISLSHA DFLKKCRTLP
     IFSQLIKLCI DGKEEFALTK EIQKHPVSGA VSHVDFQFVD RGAEIKVEVP LVFLNEQKCA
     GVKLGGALNI LHRSLLIRCA PDAIPQSLEV DLLDLAIGHS IHVSDLALPE TMQVAMKEEN
     PVIASVSATA AVEEAKEDGA PEESAQGQGA AEAQETNK