ID A0A081KEI8_9GAMM Unreviewed; 792 AA.
AC A0A081KEI8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=GV64_19160 {ECO:0000313|EMBL:KEI72564.1};
OS Endozoicomonas elysicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=305900 {ECO:0000313|EMBL:KEI72564.1, ECO:0000313|Proteomes:UP000027997};
RN [1] {ECO:0000313|EMBL:KEI72564.1, ECO:0000313|Proteomes:UP000027997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22380 {ECO:0000313|EMBL:KEI72564.1,
RC ECO:0000313|Proteomes:UP000027997};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-2014) 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:KEI72564.1}.
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DR EMBL; JOJP01000001; KEI72564.1; -; Genomic_DNA.
DR RefSeq; WP_020584930.1; NZ_JOJP01000001.1.
DR AlphaFoldDB; A0A081KEI8; -.
DR STRING; 305900.GV64_19160; -.
DR eggNOG; COG0072; Bacteria.
DR Proteomes; UP000027997; 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: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:UP000027997};
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..147
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT DOMAIN 400..476
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT DOMAIN 698..791
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT BINDING 454
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 460
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 463
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 464
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 792 AA; 86342 MW; D83648AF90E1ECA9 CRC64;
MKFSEKWLRQ WVNIEVDTQE LVDKITMAGL EVDDVESVAG EFTGVVIGEI VACEQHPDAD
KLRVTQVSTG NESFQVVCGA PNARVGIKVP FATVGAVLPG NFKIKKAKLR GVESLGMLCA
EEELGMAESS DGLMELPLDA PVGQDIREYL SLDDKIIDVD LTPNRGDCLS IAGLAREVSA
NFLADVTEEQ VVAVAPAIDD TFSVHIDAPQ GCPRYVGRVV RNVDVSRSAP LWLTERLRRS
GIRSIDPVVD VTNYVMLELG QPMHGFDLDT LSGSIHVRMA KTEEKLTLLD GQEVTLNDNT
LVIADDQKAL AIAGVMGGEG SGVSENTRNI FLESAFFDPI TIAGKARSYG LHTDSSHRFE
RGVDFQLQKK AVERATALIV EICGGEPGPV TEVASEAYLP ALREVALRSE KVTSLLGMAI
ENSHIEALLS RLGLGLTSDG EGCWKVSVPS WRFDISIEED LVEELGRIYG YNNLPESTPT
ALLKMKQVDE SLVQESDIRR VLTARGYQEA VCFSFIAPEL HKLFDPEHEA VALSNPIASD
LSVMRTTLLP GLVKTAGYNL NRQQSRVRLF ETGLTFVKEG DELKQEPMLA ALITGSRHPE
SWQDKAESVD FFDLKGDIEA VFELGLAGNE FTFHKGEHPA MHPGQCAEVV RAGNVIGHMG
ALHPSLAKKL DMPGGVYLVE LNLKAVTEGK VAGFSALSKY PEVRRDLALV VEASAAAGDI
EQLIKSEAGE LLRRVNTFDV YAGKGIEEGC KSLAMGLTLQ HPSRTLKDDE VNKLVDRVVT
RLKQEFNASL RK
//
