ID SYFB_ECOLI Reviewed; 795 AA. AC P07395; Q59407; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 24-JAN-2024, entry version 198. 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=b1713, JW1703; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2991205; DOI=10.1128/jb.163.2.787-791.1985; RA Mechulman Y., Fayat G., Blanquet S.; RT "Sequence of the Escherichia coli pheST operon and identification of the RT himA gene."; RL J. Bacteriol. 163:787-791(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Miller H.I.; RL Submitted (NOV-1986) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC -!- INTERACTION: CC P07395; P32715: mdtO; NbExp=4; IntAct=EBI-555713, EBI-555775; CC P07395; P08312: pheS; NbExp=9; IntAct=EBI-555713, EBI-555676; CC P07395; P07395: pheT; NbExp=2; IntAct=EBI-555713, EBI-555713; CC P07395; P0AG90: secD; NbExp=4; IntAct=EBI-555713, EBI-555724; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit CC family. Type 1 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V00291; CAA23565.1; -; Genomic_DNA. DR EMBL; K02844; AAA51470.1; -; Genomic_DNA. DR EMBL; U00096; AAC74783.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15481.1; -; Genomic_DNA. DR PIR; I41284; SYECFB. DR RefSeq; NP_416228.1; NC_000913.3. DR RefSeq; WP_000672380.1; NZ_SSZK01000001.1. DR PDB; 3PCO; X-ray; 3.02 A; B/D=1-795. DR PDB; 6OZ5; X-ray; 2.50 A; B/D=1-795. DR PDB; 6P24; X-ray; 2.12 A; B/D=1-795. DR PDB; 6P26; X-ray; 3.16 A; B/D=1-795. DR PDBsum; 3PCO; -. DR PDBsum; 6OZ5; -. DR PDBsum; 6P24; -. DR PDBsum; 6P26; -. DR AlphaFoldDB; P07395; -. DR SMR; P07395; -. DR BioGRID; 4262088; 218. DR BioGRID; 849758; 4. DR ComplexPortal; CPX-5222; Phenylalanyl-tRNA synthetase complex. DR DIP; DIP-6879N; -. DR IntAct; P07395; 12. DR STRING; 511145.b1713; -. DR BindingDB; P07395; -. DR DrugCentral; P07395; -. DR jPOST; P07395; -. DR PaxDb; 511145-b1713; -. DR EnsemblBacteria; AAC74783; AAC74783; b1713. DR GeneID; 945382; -. DR KEGG; ecj:JW1703; -. DR KEGG; eco:b1713; -. DR PATRIC; fig|1411691.4.peg.544; -. DR EchoBASE; EB0704; -. DR eggNOG; COG0072; Bacteria. DR eggNOG; COG0073; Bacteria. DR HOGENOM; CLU_016891_0_0_6; -. DR InParanoid; P07395; -. DR OMA; ISYNWLK; -. DR OrthoDB; 9805455at2; -. DR PhylomeDB; P07395; -. DR BioCyc; EcoCyc:PHET-MONOMER; -. DR BioCyc; MetaCyc:PHET-MONOMER; -. DR SABIO-RK; P07395; -. DR PRO; PR:P07395; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IDA:ComplexPortal. DR CDD; cd00769; PheRS_beta_core; 1. DR CDD; cd02796; tRNA_bind_bactPheRS; 1. DR Gene3D; 3.30.56.10; -; 2. DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1. DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR005146; B3/B4_tRNA-bd. DR InterPro; IPR009061; DNA-bd_dom_put_sf. DR InterPro; IPR005121; Fdx_antiC-bd. DR InterPro; IPR036690; Fdx_antiC-bd_sf. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu. DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact. DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4. DR InterPro; IPR041616; PheRS_beta_core. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR033714; tRNA_bind_bactPheRS. DR InterPro; IPR005147; tRNA_synthase_B5-dom. DR NCBIfam; TIGR00472; pheT_bact; 1. DR PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1. DR PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 1. DR Pfam; PF03483; B3_4; 1. DR Pfam; PF03484; B5; 1. DR Pfam; PF03147; FDX-ACB; 1. DR Pfam; PF01588; tRNA_bind; 1. DR Pfam; PF17759; tRNA_synthFbeta; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SMART; SM00896; FDX-ACB; 1. DR SUPFAM; SSF54991; Anticodon-binding domain of PheRS; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF56037; PheT/TilS domain; 1. DR SUPFAM; SSF46955; Putative DNA-binding domain; 1. DR PROSITE; PS51483; B5; 1. DR PROSITE; PS51447; FDX_ACB; 1. DR PROSITE; PS50886; TRBD; 1. DR SWISS-2DPAGE; P07395; -. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; RNA-binding; tRNA-binding. FT CHAIN 1..795 FT /note="Phenylalanine--tRNA ligase beta subunit" FT /id="PRO_0000126880" FT DOMAIN 39..148 FT /note="tRNA-binding" FT DOMAIN 401..476 FT /note="B5" FT DOMAIN 701..794 FT /note="FDX-ACB" FT BINDING 454 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000250" FT BINDING 460 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000250" FT BINDING 463 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000250" FT BINDING 464 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000250" FT CONFLICT 93 FT /note="A -> T (in Ref. 1; CAA23565)" FT /evidence="ECO:0000305" FT CONFLICT 141..142 FT /note="AP -> VR (in Ref. 1; CAA23565)" FT /evidence="ECO:0000305" FT CONFLICT 186..189 FT /note="PLVQ -> AAGN (in Ref. 1; CAA23565)" FT /evidence="ECO:0000305" FT CONFLICT 481 FT /note="A -> R (in Ref. 1; CAA23565)" FT /evidence="ECO:0000305" FT CONFLICT 698 FT /note="R -> G (in Ref. 1; CAA23565)" FT /evidence="ECO:0000305" FT STRAND 2..4 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 5..9 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 18..27 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 32..39 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 43..55 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 75..79 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 89..99 FT /evidence="ECO:0007829|PDB:6P24" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 113..119 FT /evidence="ECO:0007829|PDB:6P24" FT TURN 122..126 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 147..150 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 156..160 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 172..182 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:6P24" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 214..223 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 232..239 FT /evidence="ECO:0007829|PDB:6P24" FT TURN 240..242 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 248..260 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 276..280 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 286..289 FT /evidence="ECO:0007829|PDB:6P24" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:3PCO" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 301..313 FT /evidence="ECO:0007829|PDB:6P24" FT TURN 314..316 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 317..323 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 330..337 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 340..343 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 346..349 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 355..360 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 369..384 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 392..395 FT /evidence="ECO:0007829|PDB:6P24" FT TURN 397..399 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 405..409 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 410..417 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 423..432 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 436..440 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 443..447 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 458..469 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 471..473 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 480..483 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 495..503 FT /evidence="ECO:0007829|PDB:6P24" FT TURN 504..506 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 514..516 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 518..524 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:3PCO" FT HELIX 539..541 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 546..548 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 549..560 FT /evidence="ECO:0007829|PDB:6P24" FT TURN 561..563 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 568..578 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 583..585 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 586..603 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 605..607 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 614..626 FT /evidence="ECO:0007829|PDB:6P24" FT TURN 627..629 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 631..633 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 634..638 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 644..654 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 657..665 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 667..672 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 679..685 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 686..689 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 706..715 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 720..729 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 733..744 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 753..762 FT /evidence="ECO:0007829|PDB:6P24" FT STRAND 765..767 FT /evidence="ECO:0007829|PDB:6P24" FT HELIX 771..788 FT /evidence="ECO:0007829|PDB:6P24" SQ SEQUENCE 795 AA; 87378 MW; 3B55EC65D25937E5 CRC64; MKFSELWLRE WVNPAIDSDA LANQITMAGL EVDGVEPVAG SFHGVVVGEV VECAQHPNAD KLRVTKVNVG GDRLLDIVCG APNCRQGLRV AVATIGAVLP GDFKIKAAKL RGEPSEGMLC SFSELGISDD HSGIIELPAD APIGTDIREY LKLDDNTIEI SVTPNRADCL GIIGVARDVA VLNQLPLVQP EIVPVGATID DTLPITVEAP EACPRYLGRV VKGINVKAPT PLWMKEKLRR CGIRSIDAVV DVTNYVLLEL GQPMHAFDKD RIEGGIVVRM AKEGETLVLL DGTEAKLNAD TLVIADHNKA LAMGGIFGGE HSGVNDETQN VLLECAFFSP LSITGRARRH GLHTDASHRY ERGVDPALQH KAMERATRLL IDICGGEAGP VIDITNEATL PKRATITLRR SKLDRLIGHH IADEQVTDIL RRLGCEVTEG KDEWQAVAPS WRFDMEIEED LVEEVARVYG YNNIPDEPVQ ASLIMGTHRE ADLSLKRVKT LLNDKGYQEV ITYSFVDPKV QQMIHPGVEA LLLPSPISVE MSAMRLSLWT GLLATVVYNQ NRQQNRVRIF ESGLRFVPDT QAPLGIRQDL MLAGVICGNR YEEHWNLAKE TVDFYDLKGD LESVLDLTGK LNEVEFRAEA NPALHPGQSA AIYLKGERIG FVGVVHPELE RKLDLNGRTL VFELEWNKLA DRVVPQAREI SRFPANRRDI AVVVAENVPA ADILSECKKV GVNQVVGVNL FDVYRGKGVA EGYKSLAISL ILQDTSRTLE EEEIAATVAK CVEALKERFQ ASLRD //