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SYFB_YERPE
ID   SYFB_YERPE              Reviewed;         795 AA.
AC   Q8ZDX1; Q0WE97;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00283};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00283};
GN   Name=pheT {ECO:0000255|HAMAP-Rule:MF_00283};
GN   OrderedLocusNames=YPO2428, y1909, YP_2215;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00283};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00283};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00283};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00283}.
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DR   EMBL; AL590842; CAL21055.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM85476.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS62421.1; -; Genomic_DNA.
DR   PIR; AD0296; AD0296.
DR   RefSeq; WP_002211831.1; NZ_WUCM01000025.1.
DR   RefSeq; YP_002347391.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZDX1; -.
DR   SMR; Q8ZDX1; -.
DR   STRING; 214092.YPO2428; -.
DR   PaxDb; Q8ZDX1; -.
DR   DNASU; 1146856; -.
DR   EnsemblBacteria; AAM85476; AAM85476; y1909.
DR   EnsemblBacteria; AAS62421; AAS62421; YP_2215.
DR   GeneID; 57976249; -.
DR   KEGG; ype:YPO2428; -.
DR   KEGG; ypk:y1909; -.
DR   KEGG; ypm:YP_2215; -.
DR   PATRIC; fig|214092.21.peg.2836; -.
DR   eggNOG; COG0072; Bacteria.
DR   eggNOG; COG0073; Bacteria.
DR   HOGENOM; CLU_016891_0_0_6; -.
DR   OMA; ISYNWLK; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; 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..795
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000126993"
FT   DOMAIN          39..148
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          401..476
FT                   /note="B5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          701..794
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         454
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         463
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   CONFLICT        378
FT                   /note="R -> H (in Ref. 3; AAS62421)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   795 AA;  87030 MW;  1B7004524F2760A2 CRC64;
     MKFSELWLRE WVNPAISSDD LAHQITMAGL EVDGVDAVAG EFNGVVVGHV VECGQHPNAD
     KLRVTKIDVG GDRLLDIVCG APNCRQGLKV AVATVGAVLP GDFKIKAAKL RGESSEGMLC
     SFSELAISDD HDGIIELPAD APIGVDVREY LHLDDKTIEI SVTPNRADCL GIIGVARDVA
     VVNQLPLTEP DMAEVVASIN DTLPIRVDAP QACPRYLGRV VKGINVKAAT PLWMREKLRR
     CGIRSIDPVV DVTNFVLLEL GQPMHAFDLD RISGGVIVRL ATDGEELTLL DGTKAKLNAD
     TLVIADHQKP LAMAGIFGGE HSGVNEETRN VLLESAFFNP LSITGRARRH GLHTDASHRY
     ERGVDPALQH KAIERATRLL IDICGGEAGP VVDVTTASEL PKQATITLRR EKLDRLIGHH
     IPSEQVSDIL RRLGCKVTEC GSDWQAVAPS WRFDMAIEED LVEEVARIYG YNNIPDVPVR
     ADLVMTKHRE ASLSLKRVKT ALVDRGYQEA ITYSFVDPKV QALLHPQQEA LILPNPISVD
     MSAMRLSLLT GLLSAVVYNQ NRQQSRLRLF ESGLRFVPDN TADLGIRQDV MLAGVIAGHR
     YDEHWDLARQ PIDFYDLKGD LEAILELTGK LSDVQFRAEA HSALHPGQSA AIYLAGEHIG
     FIGVVHPELE RKLDLNGRTV VFEVQWNKLA DRAVPQAREI SRFPANRRDI AVVVAENVPA
     EDILAECKKV GANQVVGVNL FDVYSGKGVA EGYKSLAISL VLQDTARTLE EEEIAATVAK
     CVEALKQRFQ ASLRD
 
 
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