SYFB_PSEAE
ID SYFB_PSEAE Reviewed; 792 AA.
AC Q9I0A4;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=PA2739;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG06127.1; -; Genomic_DNA.
DR PIR; A83303; A83303.
DR RefSeq; NP_251429.1; NC_002516.2.
DR RefSeq; WP_003114408.1; NZ_QZGE01000011.1.
DR PDB; 4P71; X-ray; 2.79 A; A/B=1-792.
DR PDB; 4P72; X-ray; 2.62 A; A/B=1-792.
DR PDB; 4P73; X-ray; 3.03 A; A/B=1-792.
DR PDB; 4P74; X-ray; 2.70 A; A/B=1-792.
DR PDB; 4P75; X-ray; 2.96 A; A/B=1-792.
DR PDBsum; 4P71; -.
DR PDBsum; 4P72; -.
DR PDBsum; 4P73; -.
DR PDBsum; 4P74; -.
DR PDBsum; 4P75; -.
DR AlphaFoldDB; Q9I0A4; -.
DR SMR; Q9I0A4; -.
DR STRING; 287.DR97_5223; -.
DR BindingDB; Q9I0A4; -.
DR PaxDb; Q9I0A4; -.
DR PRIDE; Q9I0A4; -.
DR EnsemblBacteria; AAG06127; AAG06127; PA2739.
DR GeneID; 882969; -.
DR KEGG; pae:PA2739; -.
DR PATRIC; fig|208964.12.peg.2864; -.
DR PseudoCAP; PA2739; -.
DR HOGENOM; CLU_016891_0_0_6; -.
DR InParanoid; Q9I0A4; -.
DR OMA; ISYNWLK; -.
DR PhylomeDB; Q9I0A4; -.
DR BioCyc; PAER208964:G1FZ6-2778-MON; -.
DR Proteomes; UP000002438; 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 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..792
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000126932"
FT DOMAIN 39..147
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 400..476
FT /note="B5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT DOMAIN 698..791
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 STRAND 2..4
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 43..55
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 171..182
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 354..361
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 422..431
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 458..469
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 495..504
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 518..524
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 549..560
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 567..578
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:4P74"
FT STRAND 584..598
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 611..622
FT /evidence="ECO:0007829|PDB:4P72"
FT TURN 623..625
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 631..635
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 641..651
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 654..662
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 664..669
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 676..682
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 683..685
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 703..712
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 717..727
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 732..741
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 743..746
FT /evidence="ECO:0007829|PDB:4P73"
FT STRAND 750..759
FT /evidence="ECO:0007829|PDB:4P72"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:4P72"
FT HELIX 768..786
FT /evidence="ECO:0007829|PDB:4P72"
SQ SEQUENCE 792 AA; 86800 MW; 118328D5656EAE76 CRC64;
MKFSEKWLRS WANPQVSHDE LVARLSMVGL EVDADLPVAG AFSGVVVGEV LSTEQHPDAD
KLRVCQVSNG SETFQVVCGA PNVRAGLKIP FAMIGAELPD DFKIKKAKLR GVESFGMLCS
AKELQISEEN AGLLELPADA PVGQDVRTYL ELADYTIEVG LTPNRGDCLS LAGLAREVSA
IYDVPLAPVA VDAVAAQHDE TRPVELAAPA ACPRYLGRVI RNVDLSRPTP LWMVERLRRS
DIRSIDPVVD VTNYVMIELG QPMHAFDLAE INGGVRVRMA EDGEKLVLLD GQEITLRADT
LVIADHQRAL AIAGVMGGEH SGVSDSTRDL FLEAAFFDTI ALAGKARSYG LHTDSSHRFE
RGVDSQLARK AMERATRLIL DIVGGEPGPI VEQVSEAHLP KVAPITLRAE RVTQMLGMPL
DAAEIVRLLQ ALELTVVADG EGQWSVGVPS HRFDISLEVD LIEELARLYG YNRLPVRYPQ
ARLAPNNKPE ARAALPLLRR LLVARGYQEA ITFSFIDPAL FELFDPGTQP LTLANPISAD
MAAMRSSLWP GLVKALQHNL NRQQSRVRLF ESGLRFVGQL EGLKQEAMLA GAICGKRLPE
GWANGRDGVD FFDAKADVEA VLASAGALGD FSFVPGEHPA LHPGQTARIE REGRLVGYLG
ALHPELAKKL DLEQPVFLFE LLLAEVVDGH LPKFRELSRF PEVRRDLALL VDQDVPAQDI
LTQIRAAAGE WLTDLRLFDV YHGKGIDPHR KSLAVGLTWQ HPSRTLNDDE VNSTTQNIVT
SLEERFNATL RK
