SYFB_MYCPN
ID SYFB_MYCPN Reviewed; 805 AA.
AC P75563;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE Short=PheRS;
GN Name=pheT; OrderedLocusNames=MPN_106; ORFNames=MP048;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000305}.
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; U00089; AAB95696.1; -; Genomic_DNA.
DR PIR; S73374; S73374.
DR RefSeq; NP_109794.1; NC_000912.1.
DR RefSeq; WP_010874463.1; NC_000912.1.
DR AlphaFoldDB; P75563; -.
DR SMR; P75563; -.
DR IntAct; P75563; 6.
DR STRING; 272634.MPN_106; -.
DR EnsemblBacteria; AAB95696; AAB95696; MPN_106.
DR KEGG; mpn:MPN_106; -.
DR PATRIC; fig|272634.6.peg.112; -.
DR HOGENOM; CLU_016891_2_0_14; -.
DR OMA; ISYNWLK; -.
DR BioCyc; MPNE272634:G1GJ3-182-MON; -.
DR Proteomes; UP000000808; 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; cd00769; PheRS_beta_core; 1.
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..805
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126915"
FT DOMAIN 40..162
FT /note="tRNA-binding"
FT DOMAIN 412..486
FT /note="B5"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
SQ SEQUENCE 805 AA; 91714 MW; 937B7614E789547A CRC64;
MLISKKTLAV LIPEITHVSN NEICEKLQQI GIEVEAIRAF KNPDYLQLGI LRAVTPHPHD
NHLYVCQVQI DKNKQLNVVT GAVNIVDPNN LNKHVIVAKK GAELLNGLII KTKNIKGIIS
DGMLCSYVDI NPFSKHLIAD GDDTHAIVLD NINRDEFGDY LSFLNLDDVV FEVTLPTNRS
DLQSLIFLAK ELAAVLKRPV FLEQKTTMTL REFYRFPLNL RNRAQANFFG GLFLRDVAIT
SSPWTTKGLL INQELRPVNC FVDQANMVTV YTGQPIHCHD ADKIHGSVEL KLATQLETML
ALDNKEYEIK PGDLVVADEQ GTIAIVGIIG SKRTMVDNTT NNIFFEVVNY NHERIKQTAQ
RLGVANFASR LMSKPISLQA TENCLNYLQN NFLNPESIGK ISKFSSTIKA PAFNRKIYLN
FNQLRELIGV TKKQLNDHMI RNYLTSLGFK MENQIARAPA YRQDITVWQD ISEELLKILD
LNKIKEDEIL SSTKLEKHEK LNAYDALQKL RTKLQTLGFH NVITYQLISP ERARNFNLFG
LSNLWEIKNP LSNERSVLRV GLIDSLLRVI QKNAAYKNKL GNIFEFSFVK TKDSNQLHIA
ALWLEKMFGS TYQKDQGVSV DIPAMKGLAQ LIISNFGFNC DFEPITEGEY FTKNVGLKLV
VFNEQIGYVG LIKDELLAPY DLKGRPVYGL EINLDRLLNS LNRLERSYTP ISKLQDVFKD
ITFSFPRDES HFETFVKAIK KLQTIFKWEL ISVFDTEKDG VPITKYTVRY YLKNFTNTPL
TLEQIKAVET QLKQQCELAK IALDL
