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Database: UniProt
Entry: H4GI50_9LACO
LinkDB: H4GI50_9LACO
Original site: H4GI50_9LACO 
ID   H4GI50_9LACO            Unreviewed;       810 AA.
AC   H4GI50;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 62.
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   ORFNames=PS3_9429 {ECO:0000313|EMBL:EHS87389.1};
OS   Limosilactobacillus gastricus PS3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=1144300 {ECO:0000313|EMBL:EHS87389.1, ECO:0000313|Proteomes:UP000004567};
RN   [1] {ECO:0000313|EMBL:EHS87389.1, ECO:0000313|Proteomes:UP000004567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PS3 {ECO:0000313|EMBL:EHS87389.1,
RC   ECO:0000313|Proteomes:UP000004567};
RX   PubMed=23846278;
RA   Martin V., Cardenas N., Jimenez E., Maldonado A., Rodriguez J.M.,
RA   Fernandez L.;
RT   "Genome Sequence of Lactobacillus gastricus PS3, a Strain Isolated from
RT   Human Milk.";
RL   Genome Announc. 1:E00489-E00413(2013).
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:EHS87389.1}.
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DR   EMBL; AICN01000013; EHS87389.1; -; Genomic_DNA.
DR   RefSeq; WP_007121734.1; NZ_AICN01000013.1.
DR   AlphaFoldDB; H4GI50; -.
DR   STRING; 1144300.PS3_9429; -.
DR   PATRIC; fig|1144300.3.peg.195; -.
DR   OrthoDB; 9805455at2; -.
DR   Proteomes; UP000004567; 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:UP000004567};
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          42..157
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
FT   DOMAIN          412..488
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
FT   DOMAIN          717..810
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51447"
FT   BINDING         466
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         472
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         475
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         476
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   810 AA;  90024 MW;  7D91BB6278600D31 CRC64;
     MNLSYQWLNE YLPLADHQIE PAELAEKLAR TSVEIDDVYS PSTGLSKLVV GYIESCQPHP
     ESDHLKLCQV QISSEEKVQI VCGAPNVTAG KKVIVALPGA RVADNQKIRK GKIRGEVSNG
     MLCALQEIGF SEKVAPKDYE EGIWFMADDA QVGDSVFPYL GMDDTIIATD VTPNRGDMFS
     VYGNVNDIAA MYDLPVNFSM HTVEESSAEK TTDLLQVEIP DPELAPTYKA RVIKNVTIQD
     SPMWLQIRLW NAGVRPINNV VDVTNYILLK YGQPLHSFDF DKLNQKHLTV RHAQADEHLV
     TLDGEDRELT SQDLVVADGD HPVALAGTMG GDDSKIDDQT INVVLESAIF DPILVRKQAR
     CLDLHSESSM RFERGINPAM CEQALNEAAY WLQELAGGQA TQGIATGSEK VARDVNIDLS
     LTKTNDVLGT DLSMTDLQQI FKQLQFTTQV MNDDHLEVVV PPRRWDIEIQ ADLYEEIARI
     YGYDNLPSTL PATGDTEGGL TAWQKLVREA RHVLEGLGLN QAISYSLTTD EKARQFKINP
     SETAPVQLDY PMSSDHTAAR MNIISGLLND VAYNVARQVE NVALYEEGRV FLPQADQARP
     DEPEHIAMAL TGSLTTNSWL DKAQPVDFYT VKGILEQLLT NLAIAGKVSY RANDQRDEMH
     PGRTADVYLD DQLIGFLGQV HPVTAQAYKI PETYVMELDL SQLETAPRLD HHYEPISKYP
     TVTRDVALLV DQTVTNAQIV EAIQAKGGQY LVDVQLFDLY EGAHLPAGKK SLAYTLTYQD
     RQNTLTEDQV NAAFEKVVDH LQTTLAAEIR
//
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