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Database: UniProt
Entry: Q92SS9
LinkDB: Q92SS9
Original site: Q92SS9 
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   29-OCT-2014, entry version 79.
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=R00286;
GN   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). {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
CC   -!- COFACTOR: 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
CC       subunit family. Type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
CC   -!- SIMILARITY: Contains 1 B5 domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
CC   -!- SIMILARITY: Contains 1 FDX-ACB domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00283}.
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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; NYVMIEL; -.
DR   OrthoDB; EOG6CCH1J; -.
DR   BioCyc; SMEL266834:GJF6-297-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-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.
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; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54991; SSF54991; 1.
DR   SUPFAM; SSF56037; SSF56037; 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; Reference proteome; RNA-binding; tRNA-binding.
FT   CHAIN         1    808       Phenylalanine--tRNA ligase beta subunit.
FT                                /FTId=PRO_0000126937.
FT   DOMAIN       38    148       tRNA-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00283}.
FT   DOMAIN      401    476       B5. {ECO:0000255|HAMAP-Rule:MF_00283}.
FT   DOMAIN      714    807       FDX-ACB. {ECO:0000255|HAMAP-
FT                                Rule:MF_00283}.
FT   METAL       454    454       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00283}.
FT   METAL       460    460       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00283}.
FT   METAL       463    463       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00283}.
FT   METAL       464    464       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00283}.
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
//
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