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Database: UniProt
Entry: A9NEP2_ACHLI
LinkDB: A9NEP2_ACHLI
Original site: A9NEP2_ACHLI 
ID   A9NEP2_ACHLI            Unreviewed;       818 AA.
AC   A9NEP2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Large ribosomal subunit protein bL9 {ECO:0000256|HAMAP-Rule:MF_00503};
GN   Name=rplI {ECO:0000256|HAMAP-Rule:MF_00503};
GN   OrderedLocusNames=ACL_0196 {ECO:0000313|EMBL:ABX80822.1};
OS   Acholeplasma laidlawii (strain PG-8A).
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX80822.1, ECO:0000313|Proteomes:UP000008558};
RN   [1] {ECO:0000313|EMBL:ABX80822.1, ECO:0000313|Proteomes:UP000008558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-8A {ECO:0000313|EMBL:ABX80822.1,
RC   ECO:0000313|Proteomes:UP000008558};
RX   PubMed=21784942; DOI=10.1128/JB.05059-11;
RA   Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA   Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA   Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA   Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA   Ladygina V.G., Govorun V.M.;
RT   "Complete genome and proteome of Acholeplasma laidlawii.";
RL   J. Bacteriol. 193:4943-4953(2011).
CC   -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_00503}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.
CC       {ECO:0000256|ARBA:ARBA00010605, ECO:0000256|HAMAP-Rule:MF_00503}.
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DR   EMBL; CP000896; ABX80822.1; -; Genomic_DNA.
DR   RefSeq; WP_012242153.1; NC_010163.1.
DR   AlphaFoldDB; A9NEP2; -.
DR   STRING; 441768.ACL_0196; -.
DR   GeneID; 66293191; -.
DR   KEGG; acl:ACL_0196; -.
DR   eggNOG; COG0359; Bacteria.
DR   eggNOG; COG3887; Bacteria.
DR   HOGENOM; CLU_018278_0_0_14; -.
DR   OrthoDB; 9759476at2; -.
DR   Proteomes; UP000008558; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.310.30; -; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 3.10.430.100; Ribosomal protein L9, C-terminal domain; 1.
DR   Gene3D; 3.40.5.10; Ribosomal protein L9, N-terminal domain; 1.
DR   HAMAP; MF_00503; Ribosomal_L9; 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR049553; GdpP-like_PAS.
DR   InterPro; IPR000160; GGDEF_dom.
DR   InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR   InterPro; IPR020594; Ribosomal_bL9_bac/chp.
DR   InterPro; IPR020069; Ribosomal_bL9_C.
DR   InterPro; IPR036791; Ribosomal_bL9_C_sf.
DR   InterPro; IPR020070; Ribosomal_bL9_N.
DR   InterPro; IPR036935; Ribosomal_bL9_N_sf.
DR   NCBIfam; TIGR00158; L9; 1.
DR   PANTHER; PTHR47618; BIFUNCTIONAL OLIGORIBONUCLEASE AND PAP PHOSPHATASE NRNA; 1.
DR   PANTHER; PTHR47618:SF2; CYCLIC-DI-AMP PHOSPHODIESTERASE GDPP; 1.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF21370; GdpP_PAS; 1.
DR   Pfam; PF03948; Ribosomal_L9_C; 1.
DR   Pfam; PF01281; Ribosomal_L9_N; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR   SUPFAM; SSF55658; L9 N-domain-like; 1.
DR   SUPFAM; SSF55653; Ribosomal protein L9 C-domain; 1.
DR   PROSITE; PS50887; GGDEF; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008558};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_00503};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_00503};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00503};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_00503}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          185..313
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
FT   COILED          705..739
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   818 AA;  92303 MW;  E65ABC160FC335E4 CRC64;
     MRKLINGILI TLWVIAFLVF TLVTFTEMFN QIPNIKFISY MTFIVITLLA VFVLILTIVN
     NYKQYIKNLQ NRLARWSKLS PRVNQVGDDA FHELPIGILV LDEGLKEIKW VNQYAKVIFE
     GRLIDRPVAE ISASLADYLL SDNKQPITIS VKDQKYEVLY KDSFQVIYLF NVTSRENVKL
     EFIKNLPAIG ILNLDNFEDN MTNFDISEQT SIKGEYLSAI ADWVDEYNGY LKPYGDNRMV
     MLIKRKRLED MMAKKFDILE HIRDISTNYG IRVTLSIGIA SWDLEYDELS DYAQNAIELA
     EKRGGDQAVV NIQNQKIAYF GAKLESITRS SRTNARLAAQ MLGDTLNKAD QIYIMGHDQT
     DLDSFGAMIG ALKMSLTTPD IAAYLIVDME KLDPTVTDVY NYLLSMNHLV TKHVITTQEA
     LARKTKDTLL MILDTQNPQI VHSKELLDLK LKTAVIDHHR GNEASIKGDF SFIDPGASST
     VELMMELFSF FPVEIQLDAP EASVMYGGII LDTNTFTYRT NARTFDVASK LKDYGADTMM
     VKTWLRSDLN RIIKQNELLG KVEIFLDRFA IVKTEDVFND RTFIAQLSES LLEIKNVDAS
     FTIVNFSDGT VGISARSFGA INVQLLMEEM GGGGHLSSAA TQIKDVSVND AYLQLKHILE
     LEYGGDNTPM KVILLEDVKG KGKKDQVIEL AGGYANYLIS NKLAVFANEE NIKKLEDKKE
     KEREEAAKYL ELMKKVASEI EGKSITLSIN VGADGKRFGS ITTKQIVEAF HEKHGVMIDK
     KRLELANDIG SVGIYPVTVS LDKGVKATFE VNIIERRD
//
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