SYFB_HELPY
ID SYFB_HELPY Reviewed; 764 AA.
AC P56145;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=HP_0402;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000305}.
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DR EMBL; AE000511; AAD07471.1; -; Genomic_DNA.
DR PIR; B64570; B64570.
DR RefSeq; NP_207200.1; NC_000915.1.
DR RefSeq; WP_000777286.1; NC_018939.1.
DR AlphaFoldDB; P56145; -.
DR SMR; P56145; -.
DR DIP; DIP-3416N; -.
DR IntAct; P56145; 7.
DR MINT; P56145; -.
DR STRING; 85962.C694_02040; -.
DR PaxDb; P56145; -.
DR EnsemblBacteria; AAD07471; AAD07471; HP_0402.
DR KEGG; hpy:HP_0402; -.
DR PATRIC; fig|85962.47.peg.426; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR OMA; ISYNWLK; -.
DR PhylomeDB; P56145; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IBA:GO_Central.
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 HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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; 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; 2.
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; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..764
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126893"
FT DOMAIN 38..148
FT /note="tRNA-binding"
FT DOMAIN 375..455
FT /note="B5"
FT DOMAIN 673..763
FT /note="FDX-ACB"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
SQ SEQUENCE 764 AA; 85136 MW; CE182690F7B30C68 CRC64;
MKLSINDLNV FVNTPKDIAK LCEDLSRLGL EVESCIPCIA PKNVVVGKIL EKAPHKNAEK
LSVCQVDVGK EVLQIVCGAK NVAPNQFVPV ALNGALIGST TIAKTELRGV ESHGMICSSI
ELGFPKINDG ILELDESVGE LVLGKELNEY APFNTHVLEI SLTPNRGDCL SVLGIAREIS
AFYHTPLKPI KALNFTPKSG LITLSAGENI ESHLAYYLIC NHSLKTPLNI KLSLAHNNAL
SENDLNNFIE FSTHFSGVIM NAYSLNTTPM DLSVKNDENN LESVYINHQK RSTIAIKHQV
QKDLSECLLL EASYTDPISL SLKLHALKDK TLQKDNALIY RSARGSNPNL SDGLNFLSAH
LKATILESKQ TEHSLKDRTL TFQLEDITEI LGLAVEKEKI QGILKNLGFK VSVKEPNSKP
QILEVIAPNF RHDIKTIQDI AEEILRFVGI DNLVSKPLHC VSSKNSNPNY DTHRFFENLK
HKALACGFKE VIHYVFYSKE KQQKLGFEVL EDPLELQNPI TTELNTLRTS LVCGLLDASL
RNKNLGFKSI ALYEKGSVYN SKREEIQKLG FLISGLQKKE SYPDTKGKAW DFYSFAECVS
KVIGDFSLEK LTTQTPINHP YQSAKIIQNH EIIGVIAKIH PKVIQELDLF ESYYAEIDAF
KLKRPAMLLK PFSIYPSSVR DLTLIIDENT AFSGIKKALK DAQIPNLSEI LPLDIFKESN
NSIALSVRCV IHSLEKTLND EEVNSAVQKA LEILEKEFNA RLKG
