RL14_ACIB5
ID RL14_ACIB5 Reviewed; 122 AA.
AC B7IA29;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367};
GN Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367}; OrderedLocusNames=AB57_3520;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
CC -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit bridges in
CC the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and
CC together make contacts with the 16S rRNA in bridges B5 and B8.
CC {ECO:0000255|HAMAP-Rule:MF_01367}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC {ECO:0000255|HAMAP-Rule:MF_01367}.
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DR EMBL; CP001182; ACJ42887.1; -; Genomic_DNA.
DR RefSeq; WP_001982634.1; NC_011586.2.
DR PDB; 7M4V; EM; 2.54 A; J=1-122.
DR PDBsum; 7M4V; -.
DR AlphaFoldDB; B7IA29; -.
DR SMR; B7IA29; -.
DR IntAct; B7IA29; 2.
DR GeneID; 66395750; -.
DR KEGG; abn:AB57_3520; -.
DR HOGENOM; CLU_095071_2_1_6; -.
DR OMA; AKEVLCI; -.
DR Proteomes; UP000007094; Chromosome.
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 Gene3D; 2.40.150.20; -; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
DR InterPro; IPR036853; Ribosomal_L14_sf.
DR InterPro; IPR000218; Ribosomal_L14P.
DR InterPro; IPR005745; Ribosomal_L14P_bac-type.
DR InterPro; IPR019972; Ribosomal_L14P_CS.
DR PANTHER; PTHR11761; PTHR11761; 1.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SMART; SM01374; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; SSF50193; 1.
DR TIGRFAMs; TIGR01067; rplN_bact; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..122
FT /note="50S ribosomal protein L14"
FT /id="PRO_1000144206"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 12..24
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:7M4V"
SQ SEQUENCE 122 AA; 13502 MW; 2E80ED15145401F0 CRC64;
MIQTETMLDV ADNSGARRVQ CIKVLGGSHR RYASVGDIIK VTVKEAIPRA RVKKGDVMNA
VVVRTKFGIR RPDGSVIRFD DNAAVILNNN KAPIATRIFG PVTRELRTEQ FMKIISLAPE
VL
