SYFB_RICBR
ID SYFB_RICBR Reviewed; 870 AA.
AC Q1RIS8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=RBE_0655;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04736.1; -; Genomic_DNA.
DR RefSeq; WP_011477324.1; NC_007940.1.
DR AlphaFoldDB; Q1RIS8; -.
DR SMR; Q1RIS8; -.
DR STRING; 336407.RBE_0655; -.
DR PRIDE; Q1RIS8; -.
DR EnsemblBacteria; ABE04736; ABE04736; RBE_0655.
DR KEGG; rbe:RBE_0655; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_0_0_5; -.
DR OMA; ISYNWLK; -.
DR OrthoDB; 53568at2; -.
DR Proteomes; UP000001951; 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; IPR005728; Rickett_RPE.
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; 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 TIGRFAMs; TIGR01045; RPE1; 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; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..870
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000278011"
FT DOMAIN 39..148
FT /note="tRNA-binding"
FT DOMAIN 427..551
FT /note="B5"
FT DOMAIN 450..498
FT /note="RPE1 insert"
FT DOMAIN 776..869
FT /note="FDX-ACB"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
SQ SEQUENCE 870 AA; 96919 MW; 615E9C9E7B28E0E6 CRC64;
MKFTLSWLKQ FLDTSASVTE IAESLTAIGL EVEEIIDKAA DLQKFEVAYI VSTKPHPSAD
KLKICEVETK NGNLQIVCGA SNARAGIKVV LANIGVEIPN GKFKIKESNI RGEKSCGMLC
SEEELFLASE SEGIIELPED AVVGEPFTKY YGLDDPVFVI NVTPNRGDAL SVYGIARDLS
AKGIGTLKEL EIPAVKSTFS SKVKLNIKDK EACPLFTFRE IRNLKNKPSP DWLQKLLKNI
GVKPISSIVD VTNYMSYSFG QPMHAYDADK IGGGIVVDRH CEENVIPRLD CGISGEESVI
QDPVVKPRDD NRGFHALNDK KYLLNKSDLV IKDENGVQAL AGIIGGISSS CDSNTMNILL
EAACFNAKMV AASGRRLQID TDSRYRFERN IDRNFTEKAL NIATDLILSI CDGGEVSEIL
ISGEKEPAKK TLDFPAGYLE KITGIKLTIL LHNEANKGEF VGNTEHSIAA YKEVREDAST
GLTPKLPLEA SYVKGLNIKG IEAILNKLGF ATDTEKDVIK ITPPSWRHDI NILEDVVEEI
TRIYGYDKIE SIKLPELEQD NNRLREHKRI SSFKRILASK GYDEVVTNSF MNSKDAKLFT
ELKDELFLLN PISVEDNYMR PTIVPNLLDI VRKNLARSIK DMAFFEVGPN FIGLNTEATY
LTAILTGSYN SKNPHSIGRS YDIFDLKSDL ETVFDYAGLS IEKCIVSNQA TPLYYHPTRS
VNLALGKNLL GHFGQIHPKI LKHYDIKEEV FAFELNITNL PAPKAKFGKR DEFIISDYQA
NFRDYAFIIA RDQPVGEIIS YINNFNKKLV KSVILFDIYS GDKLPSGKKS IAIRVGLQAD
DRTLNEDDLN SFSKDLIANI EQKFQGTLRE
