SYFB_MALP2
ID SYFB_MALP2 Reviewed; 792 AA.
AC Q8EUJ9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00283};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00283};
GN Name=pheT {ECO:0000255|HAMAP-Rule:MF_00283}; OrderedLocusNames=MYPE9260;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00283};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00283};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC Rule:MF_00283};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00283}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00283}.
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DR EMBL; BA000026; BAC44713.1; -; Genomic_DNA.
DR RefSeq; WP_044891314.1; NC_004432.1.
DR AlphaFoldDB; Q8EUJ9; -.
DR SMR; Q8EUJ9; -.
DR STRING; 272633.26454385; -.
DR PRIDE; Q8EUJ9; -.
DR EnsemblBacteria; BAC44713; BAC44713; BAC44713.
DR KEGG; mpe:MYPE9260; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_2_0_14; -.
DR OMA; ISYNWLK; -.
DR OrthoDB; 53568at2; -.
DR Proteomes; UP000002522; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd02796; tRNA_bind_bactPheRS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 1.
DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR033714; tRNA_bind_bactPheRS.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR PANTHER; PTHR10947; PTHR10947; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00472; pheT_bact; 1.
DR PROSITE; PS51483; B5; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..792
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000232812"
FT DOMAIN 40..156
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 404..472
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
SQ SEQUENCE 792 AA; 90201 MW; 50DE4E05F302E13B CRC64;
MLLSRKLLNT LFPIFNKVSN QELETMLNSI GVEVENIIKF PRTENLIVGE IKKVEKHPNA
DKLNICEVFF ENKIHVIICG AQNVRPGLKV IVAKVGTKML DGRLIEAKDL LGVKSNGMIC
AYAELTTKTD VCSYDEIENI IELDNDAKLN DIDPLKYIGL DDEILDLSVP SNRNELNGVI
PIAYDLISLY FPKSKIDFSL KNIENQKKTS IKINIDKELC RFFGVIDVSN VEIKTSNWKI
KSFLLNCGIT PINTIVDITN LNAIITSVPC HAYDKDKLGK EIAVSLNAHK EKFLALNDKE
YVVENKSAVS VISNNKIVSL ASVIGSKENS ISNSTKNVLF EIGNFDNMAI RDASNKLGIK
TNASTLGSKT IPLWITYKSF DYLIGLLKDL NIKVSSVNYV GDKLKDNLID FDSQTIQDLL
GQKTDVEKNL KLMGFNFVGK KVKAPVYRED LENISDLVEE LTKKINVNNL ELKPIESSFV
DFEFDNFEEN WNFLEKYFIN KGFTLVKTLN LTSLENNKAF NLFGSKKSIK IMNPISSERE
YFRNNLIQQH LEVLSNNYAH KINLYNIFEI QGLNYDGLWN KHLCLTLPIE HFNNKINNSK
IVIDLLFIKS ILTDLFNVFN IPFEIKAIEN LSNDIEFIST NNGFEIYVKN KLIGIASQIS
PEILNKYKLD SSKPIYFVEL IINDLLDSKI SKSITVSDEK KEHNIARSIT LSLDRNQNYK
KIESVLDNYK NNLNLLDKFE IESVFIKDNK PSYTFSLEIN PSKLNKKETN EINEIVERLI
KDLINEGAEI KR
