SYFB_ECOLI
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 03-AUG-2022, entry version 192.
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; Proteobacteria; 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}.
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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 SWISS-2DPAGE; P07395; -.
DR jPOST; P07395; -.
DR PaxDb; P07395; -.
DR PRIDE; P07395; -.
DR EnsemblBacteria; AAC74783; AAC74783; b1713.
DR EnsemblBacteria; BAA15481; BAA15481; BAA15481.
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 PhylomeDB; P07395; -.
DR BioCyc; EcoCyc:PHET-MON; -.
DR BioCyc; MetaCyc:PHET-MON; -.
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; 2.40.50.140; -; 1.
DR Gene3D; 3.30.70.380; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 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 PANTHER; PTHR10947; PTHR10947; 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; SSF46955; SSF46955; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54991; SSF54991; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00472; pheT_bact; 1.
DR PROSITE; PS51483; B5; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
DR PROSITE; PS50886; TRBD; 1.
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
