RL22_HALSA
ID RL22_HALSA Reviewed; 156 AA.
AC P15008; P05973; Q9HPC9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
DE AltName: Full=HHal22;
DE AltName: Full=HL23;
GN Name=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=VNG_1695G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2651152; DOI=10.1016/0014-5793(89)80243-1;
RA Mankin A.S.;
RT "The nucleotide sequence of the genes coding for the S19 and L22 equivalent
RT ribosomal proteins from Halobacterium halobium.";
RL FEBS Lett. 246:13-16(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8876975; DOI=10.1080/15216549600201402;
RA Miyokawa T., Urayama T., Shimooka K., Itoh T.;
RT "Organization and nucleotide sequences of ten ribosomal protein genes from
RT the region equivalent to the S10 operon in the archaebacterium,
RT Halobacterium halobium.";
RL Biochem. Mol. Biol. Int. 39:1209-1220(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [4]
RP PROTEIN SEQUENCE OF 2-28.
RX PubMed=6467081; DOI=10.1139/o84-058;
RA Matheson A.T., Yaguchi M., Christensen P., Rollin C.F., Hasnain S.;
RT "Purification, properties, and N-terminal amino acid sequence of certain
RT 50S ribosomal subunit proteins from the archaebacterium Halobacterium
RT cutirubrum.";
RL Can. J. Biochem. Cell Biol. 62:426-433(1984).
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: The globular domain of the protein is located near the
CC polypeptide exit tunnel on the outside of the subunit, while an
CC extended beta-hairpin is found that lines the wall of the exit tunnel
CC in the center of the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000255|HAMAP-Rule:MF_01331}.
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DR EMBL; X14967; CAA33092.1; -; Genomic_DNA.
DR EMBL; AB006961; BAA22275.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19941.1; -; Genomic_DNA.
DR PIR; A84322; A84322.
DR PIR; S03883; R5HSH2.
DR RefSeq; WP_010903239.1; NC_002607.1.
DR AlphaFoldDB; P15008; -.
DR SMR; P15008; -.
DR STRING; 64091.VNG_1695G; -.
DR PaxDb; P15008; -.
DR EnsemblBacteria; AAG19941; AAG19941; VNG_1695G.
DR GeneID; 5954266; -.
DR GeneID; 62887091; -.
DR KEGG; hal:VNG_1695G; -.
DR PATRIC; fig|64091.14.peg.1293; -.
DR HOGENOM; CLU_083987_0_2_2; -.
DR InParanoid; P15008; -.
DR OMA; ANAEYKG; -.
DR OrthoDB; 103467at2157; -.
DR PhylomeDB; P15008; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR CDD; cd00336; Ribosomal_L22; 1.
DR Gene3D; 3.90.470.10; -; 1.
DR HAMAP; MF_01331_A; Ribosomal_L22_A; 1.
DR InterPro; IPR001063; Ribosomal_L22.
DR InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR InterPro; IPR005721; Ribosomal_L22/L17_euk/arc.
DR InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR PANTHER; PTHR11593; PTHR11593; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01038; uL22_arch_euk; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6467081"
FT CHAIN 2..156
FT /note="50S ribosomal protein L22"
FT /id="PRO_0000125273"
FT CONFLICT 4
FT /note="S -> F (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 13..15
FT /note="ASA -> MSR (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 17145 MW; 48DABFC4196A6286 CRC64;
MGISYSVDVD SEASAKAMLR ERSISLKHSK AIAREISGET VADAKEYLQA VIDEERSVPF
KQHNSGVGHR NDIDGWDAGR YPEKASKDFL KLLSNVSNNA DQQGFDADEM VIEHVAPHKV
GESQGRKPRA MGRATTWNAT LCDVEIVVTE TEEVTA
