ID A0A0R2L9C9_9LACO Unreviewed; 803 AA.
AC A0A0R2L9C9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283};
DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00283};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283};
DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00283};
GN Name=pheT {ECO:0000256|HAMAP-Rule:MF_00283,
GN ECO:0000313|EMBL:GEK28332.1};
GN ORFNames=IV55_GL000357 {ECO:0000313|EMBL:KRN95076.1}, LSI01_06430
GN {ECO:0000313|EMBL:GEK28332.1};
OS Furfurilactobacillus siliginis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Furfurilactobacillus.
OX NCBI_TaxID=348151 {ECO:0000313|EMBL:KRN95076.1, ECO:0000313|Proteomes:UP000051139};
RN [1] {ECO:0000313|EMBL:KRN95076.1, ECO:0000313|Proteomes:UP000051139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22696 {ECO:0000313|EMBL:KRN95076.1,
RC ECO:0000313|Proteomes:UP000051139};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
RN [2] {ECO:0000313|EMBL:GEK28332.1, ECO:0000313|Proteomes:UP000321429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101315 {ECO:0000313|EMBL:GEK28332.1,
RC ECO:0000313|Proteomes:UP000321429};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Lactobacillus siliginis NBRC 101315.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000395, ECO:0000256|HAMAP-
CC Rule:MF_00283};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00283};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC Rule:MF_00283};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00283}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000256|ARBA:ARBA00008653,
CC ECO:0000256|HAMAP-Rule:MF_00283}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRN95076.1}.
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DR EMBL; BJUD01000008; GEK28332.1; -; Genomic_DNA.
DR EMBL; JQCB01000011; KRN95076.1; -; Genomic_DNA.
DR RefSeq; WP_057811015.1; NZ_JQCB01000011.1.
DR AlphaFoldDB; A0A0R2L9C9; -.
DR STRING; 348151.IV55_GL000357; -.
DR PATRIC; fig|348151.3.peg.364; -.
DR OrthoDB; 9805455at2; -.
DR Proteomes; UP000051139; Unassembled WGS sequence.
DR Proteomes; UP000321429; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
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; 3.30.56.10; -; 2.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 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 NCBIfam; TIGR00472; pheT_bact; 1.
DR PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 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; SSF54991; Anticodon-binding domain of PheRS; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF56037; PheT/TilS domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00283};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00283}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00283};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00283};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00283};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00283}; Reference proteome {ECO:0000313|Proteomes:UP000051139};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 39..154
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT DOMAIN 408..483
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT DOMAIN 710..803
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00283"
SQ SEQUENCE 803 AA; 88149 MW; D93AE25D448F1841 CRC64;
MKVSTDWLKE YLTLDVDPQA LGEKIERTAV EVDRVYKMSD GMSKLVVGET LSVEPHPDSD
HLHVCQVNVG EEEPLQIVCG APNVATGQKV IVALPGAWIG GHNKIKKGKM RGIVSNGMLC
ALEEIGFDAK IAPGDYEDGI YILPADSKPG ESVFPILGMD DDIIETDLTP NRGDMNSMNG
TAWEIGAIYG QTPKMPEFTL TEAGNRQVTD LVTVSADAAL APTYKMRVVS GVKVQASPLW
LQKRLWEAGM RPINNIVDVT NYIMLTYGQP LHAFDYDKLA GKNVQVRLAT AGEKITTLDG
TERELRADDM VIADDKHAIA LAGTMGGLDT EIDEHTTTIA IESAIFEPIH IRKTARFFNL
HSEASMRFER GINKDDNQNA LDHAAALMAE LGNGAVEHGT VVGSDTQVAP AEVKVTLTRI
NHVLGTSLTA AEVQTIFDHL NFPTVNDGET FTVTVPARRW DIHIEADLFE EVARLFGYDN
IPSTLPYGTM TPGSLTEKQR VIRDARHLLE GAGLNQAISY ALTTTEKASQ FMLRDSEPTL
LDFPMSTDHT TTRMNLISGL LDDVAYNVAR KQANVALYEQ GRVFYRDGDE IRPVEVEHIA
GVLTGSVQDK TWNTPAKPVD FFAIKGIVNL FLHDMGLSET IRYEATSERQ EMHPGRTADI
YVGDQLVGFV GQVHPAIAAD YKVPETYVFE LNLQALIDAP HDEQQYEPIS KFPAVTRDIA
ILVDDTVTDA DILAAIHKRG GAHLASVTLF DVYEGTHLPA GKKSMAYTLT YQDATATLVE
DDVAKAFAKV EKELQTTFNA EIR
//
