SYFB_MYCTU
ID SYFB_MYCTU Reviewed; 831 AA.
AC P9WFU1; L0T8W1; P94985;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 50.
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=Rv1650; ORFNames=MTCY06H11.15;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44415.1; -; Genomic_DNA.
DR PIR; E70620; E70620.
DR RefSeq; NP_216166.1; NC_000962.3.
DR RefSeq; WP_003901220.1; NZ_NVQJ01000016.1.
DR PDB; 7DAW; X-ray; 2.83 A; B=1-831.
DR PDB; 7DB7; X-ray; 2.71 A; B=1-831.
DR PDB; 7DB8; X-ray; 2.30 A; B=1-831.
DR PDB; 7K98; X-ray; 2.19 A; B/E=1-831.
DR PDB; 7K9M; X-ray; 2.50 A; B=1-831.
DR PDB; 7KA0; X-ray; 2.40 A; B/E=1-831.
DR PDB; 7KAB; X-ray; 2.50 A; B=1-831.
DR PDBsum; 7DAW; -.
DR PDBsum; 7DB7; -.
DR PDBsum; 7DB8; -.
DR PDBsum; 7K98; -.
DR PDBsum; 7K9M; -.
DR PDBsum; 7KA0; -.
DR PDBsum; 7KAB; -.
DR AlphaFoldDB; P9WFU1; -.
DR SMR; P9WFU1; -.
DR STRING; 83332.Rv1650; -.
DR PaxDb; P9WFU1; -.
DR DNASU; 885283; -.
DR GeneID; 885283; -.
DR KEGG; mtu:Rv1650; -.
DR TubercuList; Rv1650; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR OMA; ISYNWLK; -.
DR PhylomeDB; P9WFU1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..831
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126916"
FT DOMAIN 44..155
FT /note="tRNA-binding"
FT DOMAIN 414..489
FT /note="B5"
FT DOMAIN 737..830
FT /note="FDX-ACB"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000250"
FT STRAND 1..4
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 47..61
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 128..132
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:7DB8"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:7DB8"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 350..360
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 379..394
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:7K98"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 425..430
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 471..482
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 502..516
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 532..536
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:7DB8"
FT HELIX 566..578
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 583..591
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:7DB8"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:7KA0"
FT HELIX 613..622
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 628..639
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 652..666
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 680..690
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 693..701
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 703..709
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 716..721
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 742..751
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 756..767
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 768..770
FT /evidence="ECO:0007829|PDB:7DB8"
FT STRAND 771..780
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 783..785
FT /evidence="ECO:0007829|PDB:7DB8"
FT STRAND 789..798
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:7K98"
FT HELIX 807..825
FT /evidence="ECO:0007829|PDB:7K98"
FT STRAND 828..831
FT /evidence="ECO:0007829|PDB:7DB8"
SQ SEQUENCE 831 AA; 88374 MW; 9BE010F0FA3485B2 CRC64;
MRLPYSWLRE VVAVGASGWD VTPGELEQTL LRIGHEVEEV IPLGPVDGPV TVGRVADIEE
LTGYKKPIRA CAVDIGDRQY REIICGATNF AVGDLVVVAL PGATLPGGFT ISARKAYGRN
SDGMICSAAE LNLGADHSGI LVLPPGAAEP GADGAGVLGL DDVVFHLAIT PDRGYCMSVR
GLARELACAY DLDFVDPASN SRVPPLPIEG PAWPLTVQPE TGVRRFALRP VIGIDPAAVS
PWWLQRRLLL CGIRATCPAV DVTNYVMLEL GHPMHAHDRN RISGTLGVRF ARSGETAVTL
DGIERKLDTA DVLIVDDAAT AAIGGVMGAA STEVRADSTD VLLEAAIWDP AAVSRTQRRL
HLPSEAARRY ERTVDPAISV AALDRCARLL ADIAGGEVSP TLTDWRGDPP CDDWSPPPIR
MGVDVPDRIA GVAYPQGTTA RRLAQIGAVV THDGDTLTVT PPSWRPDLRQ PADLVEEVLR
LEGLEVIPSV LPPAPAGRGL TAGQQRRRTI GRSLALSGYV EILPTPFLPA GVFDLWGLEA
DDSRRMTTRV LNPLEADRPQ LATTLLPALL EALVRNVSRG LVDVALFAIA QVVQPTEQTR
GVGLIPVDRR PTDDEIAMLD ASLPRQPQHV AAVLAGLREP RGPWGPGRPV EAADAFEAVR
IIARASRVDV TLRPAQYLPW HPGRCAQVFV GESSVGHAGQ LHPAVIERSG LPKGTCAVEL
NLDAIPCSAP LPAPRVSPYP AVFQDVSLVV AADIPAQAVA DAVRAGAGDL LEDIALFDVF
TGPQIGEHRK SLTFALRFRA PDRTLTEDDA SAARDAAVQS AAERVGAVLR G
