SYFB_STAHJ
ID SYFB_STAHJ Reviewed; 800 AA.
AC Q4L5E4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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}; OrderedLocusNames=SH1822;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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.
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; AP006716; BAE05131.1; -; Genomic_DNA.
DR RefSeq; WP_011276099.1; NC_007168.1.
DR PDB; 2RHQ; X-ray; 2.20 A; B=1-799.
DR PDB; 2RHS; X-ray; 2.20 A; B/D=1-800.
DR PDBsum; 2RHQ; -.
DR PDBsum; 2RHS; -.
DR AlphaFoldDB; Q4L5E4; -.
DR SMR; Q4L5E4; -.
DR STRING; 279808.SH1822; -.
DR DrugBank; DB07817; 1-{3-[(4-pyridin-2-ylpiperazin-1-yl)sulfonyl]phenyl}-3-(1,3-thiazol-2-yl)urea.
DR EnsemblBacteria; BAE05131; BAE05131; SH1822.
DR KEGG; sha:SH1822; -.
DR eggNOG; COG0072; Bacteria.
DR eggNOG; COG0073; Bacteria.
DR HOGENOM; CLU_016891_0_0_9; -.
DR OMA; ISYNWLK; -.
DR OrthoDB; 53568at2; -.
DR EvolutionaryTrace; Q4L5E4; -.
DR Proteomes; UP000000543; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW RNA-binding; tRNA-binding.
FT CHAIN 1..800
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000232090"
FT DOMAIN 39..154
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 408..483
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 708..800
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT BINDING 461
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 467
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 470
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 471
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 STRAND 2..4
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 43..54
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 89..99
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2RHS"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 239..247
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 255..267
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 310..321
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 363..369
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 377..391
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 409..416
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 417..424
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 465..476
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 498..512
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:2RHQ"
FT TURN 526..532
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 558..570
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 576..586
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 595..611
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 622..636
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 650..660
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 663..671
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 673..678
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 683..690
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 691..694
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 713..718
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 727..737
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 739..741
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 742..751
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 760..769
FT /evidence="ECO:0007829|PDB:2RHQ"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:2RHQ"
FT HELIX 778..794
FT /evidence="ECO:0007829|PDB:2RHQ"
SQ SEQUENCE 800 AA; 88876 MW; 7FBE75700E9AC989 CRC64;
MLISNEWLKD YVDAGVKVED LAERITRTGI EVDDMIDYSK DIKNLVVGYI QSKEKHPDAD
KLNICQVDIG EEEPVQIVCG APNVDAGQHV IVAKVGGRLP GGIKIKRAKL RGERSEGMIC
SLQEIGISSN VVPKAYENGI FVFQTEVEPG TDALTALYLN DQVMEFDLTP NRADALSMVG
TAYEVAALYQ TEMTKPETQS NETSESATNE LSVTIDNPEK VPYYSARVVK NVSIEPSPIW
VQARLIKAGI RPINNVVDIS NYVLLEYGQP LHMFDQDHIG SKEIVVRQAK DEETMTTLDN
NERKLVDTDI VISNGQEPIA LAGVMGGDFS EVTEQTTNVV IEGAIFDPVS IRHTSRRLNL
RSEASSRFEK GIATEFVDEA VDRACYLLQE LASGEVLQDR VSSGDLGSFV TPIDITAEKV
NKTIGFNLSN DEIQSIFRQL GFETTLKGET LTVNVPSRRK DITIKEDLIE EVARIYGYDE
IPSSLPVFGE VTSGELTDRQ HKTRTLKETL EGAGLNQAIT YSLVSKDHAK DFALQERPTI
SLLMPMSEAH ATLRQSLLPH LIEATAYNVA RKNKDVRLYE IGRVFFGNGE GELPDEVEYL
SGILTGEYVV NAWQGKKEEI DFFIAKGVVD RVAEKLNLEF SYKAGKIEGL HPGRTAIVSL
EGQDIGFIGE LHPQVAADND LKRTYVFELN YDAMMQVAVG YINYEQIPKF PGVTRDIALE
VNHDVPSSEL KQIIHNNGED ILQSTLVFDV YEGEHLEKGK KSVAIRLNYL DTEDTLTDER
VSKIHDKILE ALQAQGATIR
