ID SYFB_XYLFT Reviewed; 792 AA.
AC Q87AB6;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 69.
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=PD_1911;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/JB.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B.,
RA Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H.,
RA Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R.,
RA Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M.,
RA Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J.,
RA Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E.,
RA Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M.,
RA Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V.,
RA da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T.,
RA Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D.,
RA de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G.,
RA Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C.,
RA Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's
RT disease and citrus variegated chlorosis strains of Xylella
RT fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC diphosphate + L-phenylalanyl-tRNA(Phe).
CC -!- COFACTOR: Binds 2 magnesium ions per tetramer (By similarity).
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC subunit family. Type 1 subfamily.
CC -!- SIMILARITY: Contains 1 B5 domain.
CC -!- SIMILARITY: Contains 1 FDX-ACB domain.
CC -!- SIMILARITY: Contains 1 tRNA-binding domain.
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DR EMBL; AE009442; AAO29741.1; -; Genomic_DNA.
DR RefSeq; NP_780092.1; NC_004556.1.
DR ProteinModelPortal; Q87AB6; -.
DR STRING; 183190.PD1911; -.
DR EnsemblBacteria; AAO29741; AAO29741; PD_1911.
DR GeneID; 1143253; -.
DR KEGG; xft:PD1911; -.
DR PATRIC; 24152346; VBIXylFas71109_2469.
DR eggNOG; COG0073; -.
DR KO; K01890; -.
DR OMA; MKFSEQW; -.
DR ProtClustDB; PRK00629; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:HAMAP.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.56.20; -; 1.
DR Gene3D; 3.30.70.380; -; 1.
DR Gene3D; 3.50.40.10; -; 1.
DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1; -.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bac.
DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4.
DR InterPro; IPR005121; PheS_beta_Fdx_antiC-bd.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF56037; B3_4; 1.
DR SUPFAM; SSF54991; Fdx_AntiC_bd; 1.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR SUPFAM; SSF46955; Putativ_DNA_bind; 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; Complete proteome; Cytoplasm;
KW Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Protein biosynthesis; RNA-binding; tRNA-binding.
FT CHAIN 1 792 Phenylalanine--tRNA ligase beta subunit.
FT /FTId=PRO_0000126992.
FT DOMAIN 39 147 tRNA-binding.
FT DOMAIN 400 475 B5.
FT DOMAIN 698 791 FDX-ACB.
FT METAL 453 453 Magnesium (By similarity).
FT METAL 459 459 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 462 462 Magnesium (By similarity).
FT METAL 463 463 Magnesium (By similarity).
SQ SEQUENCE 792 AA; 86424 MW; CD94C012C9625516 CRC64;
MKFSENWLRN HAPIQANRDV LVATLTAIGL EVENVAVLGE ALDLILVARI VNVVPHPESD
LLQICQVDVA QDTLLQIVCG ASNVRPGLVV PLALLGAKIG ALTIKSTTLR GIESNGMLCS
AKELGLDTEA SGLMELPEDA PIGTPLADYL ALPDASIEIK LTPNRADCFS VRGIAFDVAA
ACASEVTPFH IDEIPAVSAR TLPVELHAGA NAPRYCGCVI EGIDPAAPTP VWMAERLRRS
GIRPVSLLVD ITQYVMLELG QPMHAFDVDT LRGPIGVRLS RNDEALKLLD GRTVVLDNDF
LVVTDADQPI ALAGLIGGWE TRITDTTINV FLEAAHFAPA AIMGRGRKLG LHTDASHRFE
RGVDPALPPQ AIAFATRLIL ELAGGKPGSL IHVQLPEYLP APASILLRRT RIARLLGIVI
DDAEVERILQ ALGMQVTTQA EGWRVVAPSR RFDIAIEEDL IEELVRIRGY EHLPTALPVG
ASHIAMPSET RLDMTSVRRQ LIARELQETI NYAFIDAELL RRWQLNTGQV MLMNPLSAEL
AVMRPRLLPG LVAALGRNIA RQLERVRLFE LGNVFTASDE AGAAPLETRH VAAAVCGDAF
ALQWGEQVRK VDFYDLKGDL ESLAAASGAV LTFHSSAQPW GHPGRSADVW CDDMCIGWIG
QLHPALTQTL EINVDVIAFE LALEPLVRRA LPRAHALSRF PFVRRDLACV VPEHVTWSEL
AITVRDVIGP LLRDVKLFDR YVGKGIEPGF KSLAIGLILQ DDTRTLIDRD VDDIMTKVVM
AIQQRHDVRI RS
//
