ID A0A829RWM6_9GAMM Unreviewed; 146 AA. AC A0A829RWM6; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. DE RecName: Full=50S ribosomal protein L15 {ECO:0000256|ARBA:ARBA00029547, ECO:0000256|HAMAP-Rule:MF_01341}; GN Name=rplO {ECO:0000256|HAMAP-Rule:MF_01341, GN ECO:0000313|EMBL:EXR18457.1}; GN ORFNames=J671_1324 {ECO:0000313|EMBL:EXR18457.1}; OS Acinetobacter sp. 1130196. OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=1310772 {ECO:0000313|EMBL:EXR18457.1, ECO:0000313|Proteomes:UP000020533}; RN [1] {ECO:0000313|EMBL:EXR18457.1, ECO:0000313|Proteomes:UP000020533} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1130196 {ECO:0000313|EMBL:EXR18457.1, RC ECO:0000313|Proteomes:UP000020533}; RA Harris A.D., Johnson K.J., George J., Nadendla S., Daugherty S.C., RA Parankush S., Sadzewicz L., Tallon L., Sengamalay N., Hazen T.H., RA Rasko D.A.; RT "Comparative genomics and transcriptomics to identify genetic mechanisms RT underlying the emergence of carbapenem resistant Acinetobacter baumannii RT (CRAb)."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_01341}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP- CC Rule:MF_01341}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family. CC {ECO:0000256|ARBA:ARBA00007320, ECO:0000256|HAMAP-Rule:MF_01341, CC ECO:0000256|RuleBase:RU003888}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EXR18457.1}. 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; JFWX01000011; EXR18457.1; -; Genomic_DNA. DR RefSeq; WP_002049750.1; NZ_JFWX01000011.1. DR GeneID; 60878154; -. DR Proteomes; UP000020533; Unassembled WGS sequence. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:InterPro. DR HAMAP; MF_01341; Ribosomal_L15; 1. DR InterPro; IPR036227; L18e/L15P_sf. DR InterPro; IPR030878; Ribosomal_L15. DR InterPro; IPR005749; Ribosomal_L15_bac-type. DR InterPro; IPR001196; Ribosomal_L15_CS. DR InterPro; IPR021131; Ribosomal_L18e/L15P. DR PANTHER; PTHR12934; PTHR12934; 1. DR Pfam; PF00828; Ribosomal_L27A; 1. DR SUPFAM; SSF52080; SSF52080; 1. DR TIGRFAMs; TIGR01071; rplO_bact; 1. DR PROSITE; PS00475; RIBOSOMAL_L15; 1. PE 3: Inferred from homology; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP- KW Rule:MF_01341}; KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP- KW Rule:MF_01341}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01341}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01341}. FT DOMAIN 30..145 FT /note="Ribosomal_L18e/L15P" FT /evidence="ECO:0000259|Pfam:PF00828" FT REGION 1..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..24 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 146 AA; 15481 MW; 35729AB1CEF3D324 CRC64; MTLRLNELAP AEGAKREHRR LGRGIGSGVG KTGGRGVKGQ KSRKSGGVRP GFEGGQTAIY RRLPKFGFTS QIALKTAEVR LSELTKVEGD IVSLETLKAA NVVRRDQIRA RIVLSGEITR AFTVQGVALT KGAKAAIEAA GGKVEE //