SYFB_RICPR
ID SYFB_RICPR Reviewed; 815 AA.
AC Q9ZDB4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=RP418;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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; AJ235271; CAA14875.1; -; Genomic_DNA.
DR PIR; A71700; A71700.
DR RefSeq; NP_220799.1; NC_000963.1.
DR RefSeq; WP_004599463.1; NC_000963.1.
DR AlphaFoldDB; Q9ZDB4; -.
DR SMR; Q9ZDB4; -.
DR STRING; 272947.RP418; -.
DR EnsemblBacteria; CAA14875; CAA14875; CAA14875.
DR GeneID; 57569543; -.
DR KEGG; rpr:RP418; -.
DR PATRIC; fig|272947.5.peg.431; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_0_0_5; -.
DR OMA; ISYNWLK; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
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 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..815
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126940"
FT DOMAIN 39..148
FT /note="tRNA-binding"
FT DOMAIN 421..496
FT /note="B5"
FT DOMAIN 721..814
FT /note="FDX-ACB"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
SQ SEQUENCE 815 AA; 91585 MW; F508E95333FCAE43 CRC64;
MKFTLSWLKQ FLEISASVTE IAEALTDIGL EVEEVIDKSK ELQKFEVAYI RNIKPHPSAD
KLKLCDVETK NGILQIVCGA SNVRADIKVV LANIGIEIPK GNLKIKESVI RGQKSYGMLC
SEEELLLSSN SDGIIELPKD AVVGDNFTKY YGLDDPIFVI NVTPNRGDVL GVYGIARDLS
AKGLGTLKEL ELSEIKSTFF SKIKLNVHDK EACPLFTFRE IRNLKNKPSP NWLQQLLKNV
GIKTISSLVD VTNYISHSFG QPIHAYDADK IYGGISVDCY IRSDKVISCK NHEMATAVLQ
FSNDSANFYA INGKGYLLTE NDLAIKDESG IQGLAGIIGG AKSSCNDSTT NVILEAACFN
AKMVAASGRR LKIDTDARYR NERNIDRNFT EKALNIATNL ILSICGNCEV SEVVKVGEQE
PQKKPLDFSV YFLEKITGIK LSIQEIEDIL NKLGFITDVK GDIIKVIAPS WRHDINILED
IAEEIVRIYG YDKIESIKLP ELYQNNNLRE YKRISSFKRI LASKGYDEVV TNSFMSSEDA
KLFAELKEGL FLLNPMSIEE NYMRPTVLPN LISIVSKNLA RDVKDMAFFE VGPSFVNLNI
ESTYLTAIIS GAFNNKNPHS FGRNYDIFDI KGDLEQVIEY AGLSLDKCIV IDETVLPQYY
HPTRAINIRL GKNLLGHFGQ IHPKILKYYD INQEIFAFEL NITNLPLIKA KFGKRDEFTV
SDYQANFRDY SFIVDQDHKV GEIISYIKNF NKKLVKSVML FDIYSGDKLP EGKKSIAIKI
KLQADDRTLS ETDLNSFSED LVASISQKFQ GILRE
