ID SYFB_RHIME Reviewed; 808 AA.
AC Q92SS9;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 01-MAY-2013, entry version 71.
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=R00286; ORFNames=SMc00366;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D.,
RA Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U.,
RA Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont
RT Sinorhizobium meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F.,
RA Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M.,
RA Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D.,
RA Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V.,
RA Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B.,
RA Ramsperger U., Surzycki R., Thebault P., Vandenbol M.,
RA Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; AL591688; CAC41723.1; -; Genomic_DNA.
DR RefSeq; NP_384392.1; NC_003047.1.
DR ProteinModelPortal; Q92SS9; -.
DR STRING; 266834.SMc00366; -.
DR EnsemblBacteria; CAC41723; CAC41723; SMc00366.
DR GeneID; 1231920; -.
DR KEGG; sme:SMc00366; -.
DR PATRIC; 23629773; VBISinMel96828_1656.
DR eggNOG; COG0072; -.
DR HOGENOM; HOG000292085; -.
DR KO; K01890; -.
DR OMA; MKFSEQW; -.
DR ProtClustDB; PRK00629; -.
DR BioCyc; SMEL266834:GJF6-297-MONOMER; -.
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 1 808 Phenylalanine--tRNA ligase beta subunit.
FT /FTId=PRO_0000126937.
FT DOMAIN 38 148 tRNA-binding.
FT DOMAIN 401 476 B5.
FT DOMAIN 714 807 FDX-ACB.
FT METAL 454 454 Magnesium (By similarity).
FT METAL 460 460 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 463 463 Magnesium (By similarity).
FT METAL 464 464 Magnesium (By similarity).
SQ SEQUENCE 808 AA; 86164 MW; E9634B24DD4396C8 CRC64;
MKFTLSWLKD HLETDASLEE ICARLTMIGL EVEDVDDKAA FKPFVIARVI SAEQHPNADK
LRVLMVDTGS GEPVQVVCGA PNARKGLVGA FAAPGTYVPG IGVTLSVGNI RGVESRGMMC
SEKELEISDD HTGIIDLPED APLGTSYADY AGLDDPVIEI NLTPNRPDCT SVHGIARDLA
ASGLGTLKTR PAPSFAVEGE TPVKVRLDLG EDRHLCPGFA LRLVRGVKNG PSPAWMRQRL
TAIGLRPINA LVDITNYLTF DQGRPLHVFD AAKVAGNLTV RRAREGEKVL ALDTREYTLS
PANVVIADEE GVESIGGIMG GEHSGCDENT TDVLIESALW DPMNIAKTGR TLGIITDARY
RFERGVDPEY MAPGLERATE LVLELCGGTA AKMDVVGYDG HEPRSVDFPV SEVRRLTGLE
VSSEESVSIL RKLGFGVEGS GERLTVTVPS WRPDIDGRAD LVEEVMRIHG VDNIVAAPLA
SHNAVNGKIL TTLQIRTRQA RRALATRGML EAVTWSFIPE GHAKLFGGGQ PELKLANPIA
ADMSDMRPSL LPGLLAAAQR NADKGYGDVA IFEVSGTYEG DTPEAQRRVA GGVRRGTASL
NGTGRLWSNA VKGGGKPVDV FDAKADAIAV LEACGVPMAN VQFEAGGPAW YHPGRSGTIK
LGPKIVLGAF GEFHPKTLDA LDVSGPLAGF EIYIDAMPEP KKKATRTKPA LELSPFQAVK
RDFAFVVDKG VEAAAIVRAA SGADRKLITA VNVFDVFEGA SLGEGRKSVA IEVTIQPVER
TLTDEDFEAL TARIVANVAK STGGVLRA
//
