SYFB_CHLTR
ID SYFB_CHLTR Reviewed; 790 AA.
AC O84481;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=CT_475;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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}.
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DR EMBL; AE001273; AAC68075.1; -; Genomic_DNA.
DR PIR; H71509; H71509.
DR RefSeq; NP_219988.1; NC_000117.1.
DR RefSeq; WP_010725208.1; NC_000117.1.
DR AlphaFoldDB; O84481; -.
DR SMR; O84481; -.
DR STRING; 813.O172_02605; -.
DR EnsemblBacteria; AAC68075; AAC68075; CT_475.
DR GeneID; 884251; -.
DR KEGG; ctr:CT_475; -.
DR PATRIC; fig|272561.5.peg.514; -.
DR HOGENOM; CLU_016891_0_0_0; -.
DR InParanoid; O84481; -.
DR OMA; ISYNWLK; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd00769; PheRS_beta_core; 1.
DR CDD; cd02796; tRNA_bind_bactPheRS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.70.380; -; 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; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_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; PF03484; B5; 1.
DR Pfam; PF03147; FDX-ACB; 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 SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54991; SSF54991; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00472; pheT_bact; 1.
DR PROSITE; PS51483; B5; 1.
DR PROSITE; PS51447; FDX_ACB; 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..790
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126868"
FT DOMAIN 39..154
FT /note="tRNA-binding"
FT DOMAIN 404..483
FT /note="B5"
FT DOMAIN 694..790
FT /note="FDX-ACB"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
SQ SEQUENCE 790 AA; 87095 MW; 4A3B0E1A688E0F39 CRC64;
MLVPLSLLQK FFSSPLSIEE ILQACDRIGI EAECSNVFPD SLNTVVTGKI LSASPHPDAE
RLTVAIVFDG KGERQIICGA PNCRAGIIVP IALPGAKLRN ASGEITTIKK AKIRGLESQG
MCCGADELGF PHLQKAERGI FEFPADTPLG ESACMLLAGA PLECSLTPNL GHCASLLGLA
REISFLSPVS LNIPEEFSFA SLPQETSICD MHDAGACPVF YSVKISGLSC RRSPEYLQAA
LTALGQKPLN AIVDITNYVM LSLGQPLHAY DSQAVEQKSL HAATLQSAQP LTLLNQETYT
LPAGSLVVAD QHNILGLAGV MGSAASSCSE NTTEIILEAA YFQPQAVRKY QRTIQLHTEA
AYRFTRGVDP QGVLPVLHAA IHMIQSLFPD AQISPIQKIG DDSFSPLSLS VRPKTIKRLL
DIELSTAEIV AKLSSLGFQT AVEEQAVRVE VPSYRHDIQE ETDLVEEICR TTPFVQKTQK
ILPTYTPIYS LKRELTAFLA NGGLQQFFTY SLLDTEVSSL SLQESSLIPV QNSSWKLRDS
LLPGMLKSAA TNLHRQAPYV YAFEIGNVYS KEQNRYQEEE RVAILLSRQV MDDSWQGKTP
LSFYTIKGWV EKLLCQSGAS IEDFSLQPSQ HPNFHPYQQA ALYQKKHLLG IFGTLHPQLC
RKAQIKHDVV FAELSLNVLL SLKKKSGPHY VPYPIYPASS RDITITIDRD LPADLVRREL
LSFESKWLES VHIVSVYQGR DSASQSKNVS LRMVFRDHER TLSGQEIEEE YERLTALLDK
KLANIGQGNS
