ID   RL22_HALMA              Reviewed;         155 AA.
AC   P10970; Q5V1S9;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000255|HAMAP-Rule:MF_01331};
DE   AltName: Full=50S ribosomal protein L22 {ECO:0000305};
DE   AltName: Full=Hl23;
DE   AltName: Full=Hmal22;
GN   Name=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   OrderedLocusNames=rrnAC1606;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2406244; DOI=10.1016/s0021-9258(19)39729-7;
RA   Arndt E., Kroemer W., Hatakeyama T.;
RT   "Organization and nucleotide sequence of a gene cluster coding for eight
RT   ribosomal proteins in the archaebacterium Halobacterium marismortui.";
RL   J. Biol. Chem. 265:3034-3039(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-155.
RX   PubMed=3191994; DOI=10.1016/0014-5793(88)80333-8;
RA   Hatakeyama T., Hatakeyama T., Kimura M.;
RT   "The primary structures of ribosomal proteins L16, L23 and L33 from the
RT   archaebacterium Halobacterium marismortui.";
RL   FEBS Lett. 240:21-28(1988).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-27.
RX   PubMed=3196689; DOI=10.1021/bi00418a032;
RA   Walsh M.J., McDougall J., Wittmann-Liebold B.;
RT   "Extended N-terminal sequencing of proteins of archaebacterial ribosomes
RT   blotted from two-dimensional gels onto glass fiber and poly(vinylidene
RT   difluoride) membrane.";
RL   Biochemistry 27:6867-6876(1988).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=10937989; DOI=10.1126/science.289.5481.905;
RA   Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A.;
RT   "The complete atomic structure of the large ribosomal subunit at 2.4 A
RT   resolution.";
RL   Science 289:905-920(2000).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT.
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=10937990; DOI=10.1126/science.289.5481.920;
RA   Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A.;
RT   "The structural basis of ribosome activity in peptide bond synthesis.";
RL   Science 289:920-930(2000).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT.
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=11828326; DOI=10.1038/nsb758;
RA   Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K.,
RA   Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A.;
RT   "A pre-translocational intermediate in protein synthesis observed in
RT   crystals of enzymatically active 50S subunits.";
RL   Nat. Struct. Biol. 9:225-230(2002).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=11483524; DOI=10.1093/emboj/20.15.4214;
RA   Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A.;
RT   "The kink-turn: a new RNA secondary structure motif.";
RL   EMBO J. 20:4214-4221(2001).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   FOUR MACROLIDE ANTIBIOTICS.
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=12150912; DOI=10.1016/s1097-2765(02)00570-1;
RA   Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.;
RT   "The structures of four macrolide antibiotics bound to the large ribosomal
RT   subunit.";
RL   Mol. Cell 10:117-128(2002).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=12185246; DOI=10.1073/pnas.172404099;
RA   Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.;
RT   "Structural insights into peptide bond formation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER.
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=12860128; DOI=10.1016/s0022-2836(03)00668-5;
RA   Hansen J.L., Moore P.B., Steitz T.A.;
RT   "Structures of five antibiotics bound at the peptidyl transferase center of
RT   the large ribosomal subunit.";
RL   J. Mol. Biol. 330:1061-1075(2003).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT
RP   E SITE SUBSTRATES.
RX   PubMed=14561884; DOI=10.1261/rna.5120503;
RA   Schmeing T.M., Moore P.B., Steitz T.A.;
RT   "Structures of deacylated tRNA mimics bound to the E site of the large
RT   ribosomal subunit.";
RL   RNA 9:1345-1352(2003).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RX   PubMed=23695244; DOI=10.1107/s0907444913004745;
RA   Gabdulkhakov A., Nikonov S., Garber M.;
RT   "Revisiting the Haloarcula marismortui 50S ribosomal subunit model.";
RL   Acta Crystallogr. D 69:997-1004(2013).
CC   -!- FUNCTION: This protein binds specifically to 23S rRNA. It makes
CC       multiple contacts with different domains of the 23S rRNA in the
CC       assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
CC   -!- FUNCTION: Contacts all 6 domains of the 23S rRNA, helping stabilize
CC       their relative orientation. An extended beta-hairpin in the C-terminus
CC       forms part of the polypeptide exit tunnel, in which it helps forms a
CC       bend with protein L4, while most of the rest of the protein is located
CC       at the polypeptide exit tunnel on the outside of the subunit.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts the macrolide
CC       antibiotic tylosin in the polypeptide exit tunnel. {ECO:0000255|HAMAP-
CC       Rule:MF_01331, ECO:0000269|PubMed:12150912,
CC       ECO:0000269|PubMed:12860128}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01331}.
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DR   EMBL; J05222; AAA86864.1; -; Genomic_DNA.
DR   EMBL; AY596297; AAV46523.1; -; Genomic_DNA.
DR   PIR; H35063; R5HS22.
DR   RefSeq; WP_011223742.1; NZ_CP039138.1.
DR   PDB; 1FFK; X-ray; 2.40 A; O=2-155.
DR   PDB; 1JJ2; X-ray; 2.40 A; Q=2-155.
DR   PDB; 1K73; X-ray; 3.01 A; S=2-155.
DR   PDB; 1K8A; X-ray; 3.00 A; S=2-155.
DR   PDB; 1K9M; X-ray; 3.00 A; S=2-155.
DR   PDB; 1KC8; X-ray; 3.01 A; S=2-155.
DR   PDB; 1KD1; X-ray; 3.00 A; S=2-155.
DR   PDB; 1KQS; X-ray; 3.10 A; Q=2-155.
DR   PDB; 1M1K; X-ray; 3.20 A; S=2-155.
DR   PDB; 1M90; X-ray; 2.80 A; S=2-155.
DR   PDB; 1N8R; X-ray; 3.00 A; S=2-155.
DR   PDB; 1NJI; X-ray; 3.00 A; S=2-155.
DR   PDB; 1Q7Y; X-ray; 3.20 A; S=2-155.
DR   PDB; 1Q81; X-ray; 2.95 A; S=2-155.
DR   PDB; 1Q82; X-ray; 2.98 A; S=2-155.
DR   PDB; 1Q86; X-ray; 3.00 A; S=2-155.
DR   PDB; 1QVF; X-ray; 3.10 A; Q=2-155.
DR   PDB; 1QVG; X-ray; 2.90 A; Q=2-155.
DR   PDB; 1S72; X-ray; 2.40 A; R=1-155.
DR   PDB; 1VQ4; X-ray; 2.70 A; R=1-155.
DR   PDB; 1VQ5; X-ray; 2.60 A; R=1-155.
DR   PDB; 1VQ6; X-ray; 2.70 A; R=1-155.
DR   PDB; 1VQ7; X-ray; 2.50 A; R=1-155.
DR   PDB; 1VQ8; X-ray; 2.20 A; R=1-155.
DR   PDB; 1VQ9; X-ray; 2.40 A; R=1-155.
DR   PDB; 1VQK; X-ray; 2.30 A; R=1-155.
DR   PDB; 1VQL; X-ray; 2.30 A; R=1-155.
DR   PDB; 1VQM; X-ray; 2.30 A; R=1-155.
DR   PDB; 1VQN; X-ray; 2.40 A; R=1-155.
DR   PDB; 1VQO; X-ray; 2.20 A; R=1-155.
DR   PDB; 1VQP; X-ray; 2.25 A; R=1-155.
DR   PDB; 1W2B; X-ray; 3.50 A; Q=2-155.
DR   PDB; 1YHQ; X-ray; 2.40 A; R=1-155.
DR   PDB; 1YI2; X-ray; 2.65 A; R=1-155.
DR   PDB; 1YIJ; X-ray; 2.60 A; R=1-155.
DR   PDB; 1YIT; X-ray; 2.80 A; R=1-155.
DR   PDB; 1YJ9; X-ray; 2.80 A; R=1-152.
DR   PDB; 1YJN; X-ray; 3.00 A; R=1-155.
DR   PDB; 1YJW; X-ray; 2.90 A; R=1-155.
DR   PDB; 2OTJ; X-ray; 2.90 A; R=1-155.
DR   PDB; 2OTL; X-ray; 2.70 A; R=1-155.
DR   PDB; 2QA4; X-ray; 3.00 A; R=1-155.
DR   PDB; 2QEX; X-ray; 2.90 A; R=1-155.
DR   PDB; 3CC2; X-ray; 2.40 A; R=1-155.
DR   PDB; 3CC4; X-ray; 2.70 A; R=1-155.
DR   PDB; 3CC7; X-ray; 2.70 A; R=1-155.
DR   PDB; 3CCE; X-ray; 2.75 A; R=1-155.
DR   PDB; 3CCJ; X-ray; 2.70 A; R=1-155.
DR   PDB; 3CCL; X-ray; 2.90 A; R=1-155.
DR   PDB; 3CCM; X-ray; 2.55 A; R=1-155.
DR   PDB; 3CCQ; X-ray; 2.90 A; R=1-155.
DR   PDB; 3CCR; X-ray; 3.00 A; R=1-155.
DR   PDB; 3CCS; X-ray; 2.95 A; R=1-155.
DR   PDB; 3CCU; X-ray; 2.80 A; R=1-155.
DR   PDB; 3CCV; X-ray; 2.90 A; R=1-155.
DR   PDB; 3CD6; X-ray; 2.75 A; R=1-155.
DR   PDB; 3CMA; X-ray; 2.80 A; R=1-155.
DR   PDB; 3CME; X-ray; 2.95 A; R=1-155.
DR   PDB; 3CPW; X-ray; 2.70 A; Q=1-155.
DR   PDB; 3CXC; X-ray; 3.00 A; Q=2-155.
DR   PDB; 3G4S; X-ray; 3.20 A; R=2-151.
DR   PDB; 3G6E; X-ray; 2.70 A; R=2-151.
DR   PDB; 3G71; X-ray; 2.85 A; R=2-151.
DR   PDB; 3I55; X-ray; 3.11 A; R=1-155.
DR   PDB; 3I56; X-ray; 2.90 A; R=1-155.
DR   PDB; 3OW2; X-ray; 2.70 A; Q=2-151.
DR   PDB; 4ADX; EM; 6.60 A; R=1-155.
DR   PDB; 4V9F; X-ray; 2.40 A; R=1-155.
DR   PDBsum; 1FFK; -.
DR   PDBsum; 1JJ2; -.
DR   PDBsum; 1K73; -.
DR   PDBsum; 1K8A; -.
DR   PDBsum; 1K9M; -.
DR   PDBsum; 1KC8; -.
DR   PDBsum; 1KD1; -.
DR   PDBsum; 1KQS; -.
DR   PDBsum; 1M1K; -.
DR   PDBsum; 1M90; -.
DR   PDBsum; 1N8R; -.
DR   PDBsum; 1NJI; -.
DR   PDBsum; 1Q7Y; -.
DR   PDBsum; 1Q81; -.
DR   PDBsum; 1Q82; -.
DR   PDBsum; 1Q86; -.
DR   PDBsum; 1QVF; -.
DR   PDBsum; 1QVG; -.
DR   PDBsum; 1S72; -.
DR   PDBsum; 1VQ4; -.
DR   PDBsum; 1VQ5; -.
DR   PDBsum; 1VQ6; -.
DR   PDBsum; 1VQ7; -.
DR   PDBsum; 1VQ8; -.
DR   PDBsum; 1VQ9; -.
DR   PDBsum; 1VQK; -.
DR   PDBsum; 1VQL; -.
DR   PDBsum; 1VQM; -.
DR   PDBsum; 1VQN; -.
DR   PDBsum; 1VQO; -.
DR   PDBsum; 1VQP; -.
DR   PDBsum; 1W2B; -.
DR   PDBsum; 1YHQ; -.
DR   PDBsum; 1YI2; -.
DR   PDBsum; 1YIJ; -.
DR   PDBsum; 1YIT; -.
DR   PDBsum; 1YJ9; -.
DR   PDBsum; 1YJN; -.
DR   PDBsum; 1YJW; -.
DR   PDBsum; 2OTJ; -.
DR   PDBsum; 2OTL; -.
DR   PDBsum; 2QA4; -.
DR   PDBsum; 2QEX; -.
DR   PDBsum; 3CC2; -.
DR   PDBsum; 3CC4; -.
DR   PDBsum; 3CC7; -.
DR   PDBsum; 3CCE; -.
DR   PDBsum; 3CCJ; -.
DR   PDBsum; 3CCL; -.
DR   PDBsum; 3CCM; -.
DR   PDBsum; 3CCQ; -.
DR   PDBsum; 3CCR; -.
DR   PDBsum; 3CCS; -.
DR   PDBsum; 3CCU; -.
DR   PDBsum; 3CCV; -.
DR   PDBsum; 3CD6; -.
DR   PDBsum; 3CMA; -.
DR   PDBsum; 3CME; -.
DR   PDBsum; 3CPW; -.
DR   PDBsum; 3CXC; -.
DR   PDBsum; 3G4S; -.
DR   PDBsum; 3G6E; -.
DR   PDBsum; 3G71; -.
DR   PDBsum; 3I55; -.
DR   PDBsum; 3I56; -.
DR   PDBsum; 3OW2; -.
DR   PDBsum; 4ADX; -.
DR   PDBsum; 4V9F; -.
DR   AlphaFoldDB; P10970; -.
DR   SMR; P10970; -.
DR   IntAct; P10970; 2.
DR   STRING; 272569.rrnAC1606; -.
DR   PaxDb; 272569-rrnAC1606; -.
DR   EnsemblBacteria; AAV46523; AAV46523; rrnAC1606.
DR   GeneID; 40152572; -.
DR   KEGG; hma:rrnAC1606; -.
DR   PATRIC; fig|272569.17.peg.2296; -.
DR   eggNOG; arCOG04098; Archaea.
DR   HOGENOM; CLU_083987_0_2_2; -.
DR   EvolutionaryTrace; P10970; -.
DR   Proteomes; UP000001169; Chromosome I.
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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00336; Ribosomal_L22; 1.
DR   Gene3D; 3.90.470.10; Ribosomal protein L22/L17; 1.
DR   HAMAP; MF_01331_A; Ribosomal_uL22_A; 1.
DR   InterPro; IPR001063; Ribosomal_uL22.
DR   InterPro; IPR018260; Ribosomal_uL22_CS.
DR   InterPro; IPR005721; Ribosomal_uL22_euk/arc.
DR   InterPro; IPR036394; Ribosomal_uL22_sf.
DR   NCBIfam; TIGR01038; uL22_arch_euk; 1.
DR   PANTHER; PTHR11593; 60S RIBOSOMAL PROTEIN L17; 1.
DR   PANTHER; PTHR11593:SF10; 60S RIBOSOMAL PROTEIN L17; 1.
DR   Pfam; PF00237; Ribosomal_L22; 1.
DR   SUPFAM; SSF54843; Ribosomal protein L22; 1.
DR   PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3191994,
FT                   ECO:0000269|PubMed:3196689"
FT   CHAIN           2..155
FT                   /note="Large ribosomal subunit protein uL22"
FT                   /id="PRO_0000125272"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          14..22
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   HELIX           26..36
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   HELIX           41..52
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          74..80
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   HELIX           83..102
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   HELIX           107..109
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          110..123
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          126..128
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:1VQ8"
FT   STRAND          139..149
FT                   /evidence="ECO:0007829|PDB:1VQ8"
SQ   SEQUENCE   155 AA;  16941 MW;  E6730272296C0D7C CRC64;
     MGISYSVEAD PDTTAKAMLR ERQMSFKHSK AIAREIKGKT AGEAVDYLEA VIEGDQPVPF
     KQHNSGVGHK SKVDGWDAGR YPEKASKAFL DLLENAVGNA DHQGFDGEAM TIKHVAAHKV
     GEQQGRKPRA MGRASAWNSP QVDVELILEE PEVED
//