ID D8GSA4_CLOLD Unreviewed; 793 AA.
AC D8GSA4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 01-MAY-2013, entry version 20.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
GN Name=pheT; OrderedLocusNames=CLJU_c34410;
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55383 / DSM 13528 / PETC;
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform
RT based on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
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; CP001666; ADK16486.1; -; Genomic_DNA.
DR RefSeq; YP_003781588.1; NC_014328.1.
DR EnsemblBacteria; ADK16486; ADK16486; CLJU_c34410.
DR GeneID; 9447057; -.
DR KEGG; clj:CLJU_c34410; -.
DR PATRIC; 42488257; VBICloLju82977_3486.
DR HOGENOM; HOG000292087; -.
DR KO; K01890; -.
DR BioCyc; CLJU748727:GHMO-3440-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 DOMAIN 39 150 tRNA-binding (By similarity).
FT DOMAIN 404 479 B5 (By similarity).
FT DOMAIN 699 792 FDX-ACB (By similarity).
FT METAL 457 457 Magnesium (By similarity).
FT METAL 463 463 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 466 466 Magnesium (By similarity).
FT METAL 467 467 Magnesium (By similarity).
SQ SEQUENCE 793 AA; 89026 MW; BCBD493EC822D432 CRC64;
MKVPVKWLKD YVKIDIPGKE LGDRLTLSGS KLEEAIVTGD EIQNVVTGKI MKIESHPQAD
KLVVCQVDIG KEEPIQIITA ATNMKEQDIV PVALHDSTLH GGVKIKKGKL RGLMSNGMFC
SEEELGIAGD KPVYGLMILK EDTPIGKDIK EVLDMTSTIL DFEITSNRPD CLSIIGMARE
TAATLNESYK IPELDYKPSC SENIQDTLKV EIKDKLCKRY MARGIKDVKI EPSPSWMQER
LLEAGVRPIN NIVDITNFVM LEIGEPMHAY DVREIKSGTI VVDTAKDGEK FTTLDEEERQ
LNQDMLTIRD GDRTIGLAGI MGGLNSEIRD DTSSIVFECA NFDGTNIRVS SQKLALRTEA
SGRFEKDLDP NLAEIAMNRA CNLVEMLKAG KVMEGTIDVY DEKIEPHSVD VDSNWVNKFL
GTEIPKENMV DYLNRLELKT QLKGDILHID VPTFRGDINI REDVAEEVAR IYGYSNVPTT
VIESVSTRGG KNPKQKLDDK LVETLISSGL NQSISYSFVS RKVFDKILLP EDSKLRNAIA
IKNPLGEDYS IMRTTTLASM MECLGRNYSR KNEIVRLFEI GRVYLPLENG DTLPEEDNIV
TIGMYGECDY FNLKGIVENI LDTLGIEKIS FKRESDNPTF HPGRTAALYV NRKLAGVLGE
IHPTVCENYG IDERCYIAEL NLDVLYEHAD SDKKYRPLPK FPAVSRDLAV LVDDNIMVQE
VEDIIRKQGG NILEKVKLFD VYRGKQIESG KKSIAYSISY RAENKTLTDK EVNKVHSKII
RSLEHNLGAQ LRQ
//
