SYFB_AYWBP
ID SYFB_AYWBP Reviewed; 828 AA.
AC Q2NJZ2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=AYWB_134;
OS Aster yellows witches'-broom phytoplasma (strain AYWB).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=322098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYWB;
RX PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT "Living with genome instability: the adaptation of phytoplasmas to diverse
RT environments of their insect and plant hosts.";
RL J. Bacteriol. 188:3682-3696(2006).
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}.
CC -!- CAUTION: Lacks the conserved glutamate residue in position 506 that
CC binds magnesium; it is replaced by a serine residue. {ECO:0000305}.
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DR EMBL; CP000061; ABC65251.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2NJZ2; -.
DR SMR; Q2NJZ2; -.
DR STRING; 322098.AYWB_134; -.
DR PRIDE; Q2NJZ2; -.
DR EnsemblBacteria; ABC65251; ABC65251; AYWB_134.
DR KEGG; ayw:AYWB_134; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_0_0_14; -.
DR OMA; ISYNWLK; -.
DR PhylomeDB; Q2NJZ2; -.
DR Proteomes; UP000001934; 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; 3.30.70.380; -; 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; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..828
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000232796"
FT DOMAIN 43..161
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 436..519
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 736..828
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT REGION 203..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497
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 503
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 507
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 828 AA; 94288 MW; E466C45A5920C289 CRC64;
MQGTPTMKII ENILKNHLLQ PLSQNIFVLT NNYITEVQKF SPLSKNTNLV VGQILNFQKI
QDSQKLNLVE VNIGIKVVKI VCGASNLQNG KKVIVASEGS FLEGINSTLK NKKIYGVFSE
GMLCALEELG ISNKFLTPQE QEGIYLFDDP NDQIALGSNA LIPLGMDGFI LELGITPNRG
DLLSHIGFAK DLQAVLASQN SNKKKEKKTI NYKTKNSKDQ TNRKTTPKLN PDFFAKLPQS
PLKVQIESDS CYEYNVCILE NITIKPSPLW LRNTLLQSGI NPINNVVDIT NLILIEYGIP
LHAFDSGTIQ KIKVRKAFPQ ETITTLNQND FVLDENDLVI TDGKKAIALA GIVGLLESSI
KPTTTKIILE AAYFSPQTIA QTCQKLKNKT ESSLRFERGI DQNLIPLAFQ KACQLLVTLA
NAKITYQPTI TKQKIRTNPT ISLDLDFITR KIGFSLCPTQ IKNWLLNLDY QIHTPKNLTL
QNKNEQLNLQ APLRRYDVKI KEDVISDLTR FYGCHKLPPQ TIQIPTQGKL TLKQKNIREL
RKLLVNLGFY ETITYSLISS EMFEAFAPQK PFIKIMNPLS QDKMILRQSL LSSLVEILSY
QHKRQTFDTA FFEIGKAYFP NQEKLSLAFV LSGNFLNTLW HKQDVSSSFF VTKGILEKIS
SFLGITLTYQ KTQKHSNFHP GMQANLLFNN QIIGVIGKTH PQLNAKHHLK ESFLCELFLS
DEILNTTKTL TFRPIPKFPT VIRDLSFLVD TKYSFYQIEQ IIKQTTPFDL IKCELFDVYQ
TPTTKEKQSF ALRFFFNNLD KNLEKQDVEH CMKKITYNLI KHFRIEIR
