SYFB_BACSU
ID SYFB_BACSU Reviewed; 804 AA.
AC P17922; P94540;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 160.
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=BSU28630;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=2127701; DOI=10.1016/0300-9084(90)90157-c;
RA Brakhage A., Wozny M., Putzer H.;
RT "Structure and nucleotide sequence of the Bacillus subtilis phenylalanyl-
RT tRNA synthetase genes.";
RL Biochimie 72:725-734(1990).
RN [2]
RP ERRATUM OF PUBMED:2127701.
RX PubMed=1903307; DOI=10.1016/0300-9084(91)90085-f;
RA Brakhage A., Wozny M., Putzer H.;
RL Biochimie 73:127-127(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(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.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000305}.
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DR EMBL; X53057; CAA37225.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99564.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14823.1; -; Genomic_DNA.
DR PIR; A69676; YFBSB.
DR RefSeq; NP_390741.1; NC_000964.3.
DR RefSeq; WP_004398979.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P17922; -.
DR SMR; P17922; -.
DR IntAct; P17922; 1.
DR MINT; P17922; -.
DR STRING; 224308.BSU28630; -.
DR jPOST; P17922; -.
DR PaxDb; P17922; -.
DR PRIDE; P17922; -.
DR EnsemblBacteria; CAB14823; CAB14823; BSU_28630.
DR GeneID; 937445; -.
DR KEGG; bsu:BSU28630; -.
DR PATRIC; fig|224308.179.peg.3110; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR InParanoid; P17922; -.
DR OMA; ISYNWLK; -.
DR PhylomeDB; P17922; -.
DR BioCyc; BSUB:BSU28630-MON; -.
DR SABIO-RK; P17922; -.
DR Proteomes; UP000001570; 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 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..804
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126844"
FT DOMAIN 40..155
FT /note="tRNA-binding"
FT DOMAIN 409..484
FT /note="B5"
FT DOMAIN 710..803
FT /note="FDX-ACB"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT CONFLICT 110..111
FT /note="KL -> NV (in Ref. 1; CAA37225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 804 AA; 87945 MW; D2337DEAE639E651 CRC64;
MFVSYKWLED YVDLKGMDPA VLAEKITRAG IEVEGIEYKG EGIKGVVIGH VLEREQHPNA
DKLNKCLVDI GAEAPVQIIC GAPNVDKGQK VAVATVGAVL PGNFKIKKAK LRGEESNGMI
CSLQELGIES KLVAKEYAEG IFVFPNDAET GSDALAALQL DDAILELGLT PNRADAMNML
GVAYEVAAIL DTEVKLPQTD YPAASEQASD YISVKIEDQE ANPLYTAKII KNVTIAPSPL
WMQTKLMNAG IRPHNNVVDI TNFVLLEYGQ PLHAFDYDRF GSKEVVVRKA AENEMIVTLD
DQERKLSADH LVITNGTKAQ AVAGVMGGAE SEVQEDTKTI LLEAAYFNGQ KVRKASKDLG
LRSESSVRFE KGIDPARVRL AAERAAQLIH LYAGGEVLAG TVEEDHLTIE ANNIHVSADK
VSSVLGLTIS KEELISIYKR LGFTVGEADD LLVVTVPSRR GDITIEEDLI EEAARLYGYD
NIPSTLPETA GTTGGLTPYQ AKRRKVRRFL EGAGLSQAIT YSLTNEKKAT AFAIEKSLNT
VLALPMSEER SILRHSLVPN LLDSVSYNLA RQTDSVALYE VGSVFLTKEE DTKPVETERV
AGAVTGLWRK QLWQGEKKPV DFFVVKGIVE GLLDKLNVLD SIEFVQSERK QLHPGRTANI
LLNGSLIGFI GQVHPSLEKE LDIKETYVFE LDLHALLAAE TAPLVYTAIP KYPSVTRDIA
LVTDKTVTSG QLESVIKEAG GKLLKEVTVF DVYEGEHMEE GKKSVAFSLQ YVNPEQTLTE
EEVTKAHSKV LKALEDTYQA VLRG
