ID SYFB_CAUCR Reviewed; 799 AA.
AC Q9A9E5;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 01-MAY-2013, entry version 77.
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=CC_1043;
OS Caulobacter crescentus (strain ATCC 19089 / CB15).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H.,
RA Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J.,
RA Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J.,
RA Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L.,
RA Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(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; AE005673; AAK23027.1; -; Genomic_DNA.
DR PIR; G87378; G87378.
DR RefSeq; NP_419859.1; NC_002696.2.
DR ProteinModelPortal; Q9A9E5; -.
DR SMR; Q9A9E5; 1-798.
DR EnsemblBacteria; AAK23027; AAK23027; CC_1043.
DR GeneID; 940568; -.
DR KEGG; ccr:CC_1043; -.
DR PATRIC; 21299058; VBICauCre124313_1059.
DR eggNOG; COG0073; -.
DR HOGENOM; HOG000292085; -.
DR KO; K01890; -.
DR OMA; ELERKCK; -.
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; Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1 799 Phenylalanine--tRNA ligase beta subunit.
FT /FTId=PRO_0000126863.
FT DOMAIN 39 148 tRNA-binding.
FT DOMAIN 403 477 B5.
FT DOMAIN 706 798 FDX-ACB.
FT METAL 455 455 Magnesium (By similarity).
FT METAL 461 461 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 464 464 Magnesium (By similarity).
FT METAL 465 465 Magnesium (By similarity).
SQ SEQUENCE 799 AA; 83872 MW; 70EA95DEB73B4180 CRC64;
MKFTLSWLKD HLETTATVPE IVAAMTMAGL EVEHVIDPAT KLAPFTVCKI VEAARHPNAD
RLQVCQVDTV DGRKEIVCGA PNARPGLTTI YAPIGAYVPG LDVTLVEKPV RGVVSNGMLC
SAAELEYASE SDGIMELEGS LAVGTPAVDA LGLEAVIDFE VTPNRPDWLG VAGIARDLAA
AGVGTLKDLS IAPIAGTYPS PISVTVDGEA CPAFAGRYIR GVKNGPSPKW LQDRLTAIGL
RPINALVDVT NLISYDRARP LHVYDAHKLS GTQISTRLGR HGEHGDEHLI ALDGKTYELT
PEMCVIADAN GERPIGLGGV MGGESTGCSE DTVDVFVESA WFEPIRIAQT GRTTGIASDA
QYRFARTVDT GSLVPGIELA TKLILELCGG EPSEVVYVGE VPAAPKGFAF DPDYVGQLSG
LAVTPEKTHQ ILAALGFDVV LGSPWTVTPP TFRRDVEGKA DLVEEVARIA GYGALPSTPL
PEVPRAVGGI LTAKQARARA ARRALAAAGY AEAVTFSFTN RKTASLFGGG QDVLVLANPI
ASELDCMRPS LLPNLIEAAG RNARQGFADA ALFEIGPTFH GDKPADQRTV VSAILAPKAP
RGWDKAAQGD VFTVKADLLA LLEELGAPVA SLQTAQGSAS SWWHPGRSAR LQLGPKAVMA
EFGEIHPAVL KALDVAGPVF GFEITLEAIP EPKKKSIKTK PAFSPSALMP LTRDFAFLVE
KAKAAGDLVK AAAGADKALI TAARVFDVYE GPGVPDGFKS VAIEVVVQPR EATLTDAEIE
ALSAKVVAAA EKAGGKLRS
//
