ID A0A0I9YDF0_9MYCO Unreviewed; 193 AA.
AC A0A0I9YDF0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
GN ORFNames=ABH38_04780 {ECO:0000313|EMBL:KLO37932.1};
OS Mycobacterium haemophilum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO37932.1, ECO:0000313|Proteomes:UP000036334};
RN [1] {ECO:0000313|EMBL:KLO37932.1, ECO:0000313|Proteomes:UP000036334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA Greninger A.L., Cunningham G., Miller S.;
RT "Genome sequence of Mycobacterium haemophilum.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01331}.
CC -!- FUNCTION: This protein binds specifically to 23S rRNA; its binding is
CC stimulated by other ribosomal proteins, e.g., L4, L17, and L20. It is
CC important during the early stages of 50S assembly. It makes multiple
CC contacts with different domains of the 23S rRNA in the assembled 50S
CC subunit and ribosome. {ECO:0000256|HAMAP-Rule:MF_01331,
CC ECO:0000256|RuleBase:RU004008}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01331, ECO:0000256|RuleBase:RU004006}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000256|ARBA:ARBA00009451, ECO:0000256|HAMAP-Rule:MF_01331,
CC ECO:0000256|RuleBase:RU004005}.
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:KLO37932.1}.
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; LDPR01000003; KLO37932.1; -; Genomic_DNA.
DR RefSeq; WP_047313521.1; NZ_LDPT01000007.1.
DR AlphaFoldDB; A0A0I9YDF0; -.
DR STRING; 1202450.B586_18730; -.
DR PATRIC; fig|29311.18.peg.1712; -.
DR OrthoDB; 9805969at2; -.
DR Proteomes; UP000036334; Unassembled WGS sequence.
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_B; Ribosomal_L22_B; 1.
DR InterPro; IPR001063; Ribosomal_uL22.
DR InterPro; IPR005727; Ribosomal_uL22_bac/chlpt-type.
DR InterPro; IPR047867; Ribosomal_uL22_bac/org-type.
DR InterPro; IPR018260; Ribosomal_uL22_CS.
DR InterPro; IPR036394; Ribosomal_uL22_sf.
DR NCBIfam; TIGR01044; rplV_bact; 1.
DR PANTHER; PTHR13501:SF10; 50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC; 1.
DR PANTHER; PTHR13501; CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; Ribosomal protein L22; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000036334};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01331}.
FT REGION 117..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 193 AA; 20080 MW; 15E74D2D4E57D52C CRC64;
MTTTEFPSAF PSATAKARFV RVSPRKARRV IDLVRGRSVA DALDILRWAP QAASEPVAKV
IASAAANAQN NNGLDPATLV VATVYADEGP TAKRIRPRAQ GRAFRIRRRT SHITVVVESR
PAKDQRSAKS TRARRAEASK AAGSAPVKKA TASSAATKAP AKKAPAKKAP AKKAAASSGA
KTSEASEAKG GSD
//
