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Database: UniProt
Entry: A0A1I5BGJ9_9MICO
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Original site: A0A1I5BGJ9_9MICO 
ID   A0A1I5BGJ9_9MICO        Unreviewed;       841 AA.
AC   A0A1I5BGJ9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SAMN05216219_1877 {ECO:0000313|EMBL:SFN73854.1};
OS   Mycetocola miduiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Mycetocola.
OX   NCBI_TaxID=995034 {ECO:0000313|EMBL:SFN73854.1, ECO:0000313|Proteomes:UP000198867};
RN   [1] {ECO:0000313|Proteomes:UP000198867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.11101 {ECO:0000313|Proteomes:UP000198867};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOVM01000005; SFN73854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5BGJ9; -.
DR   STRING; 995034.SAMN05216219_1877; -.
DR   OrthoDB; 9805455at2; -.
DR   Proteomes; UP000198867; 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; 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:UP000198867};
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          40..163
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
FT   DOMAIN          421..496
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
FT   DOMAIN          747..840
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51447"
FT   BINDING         474
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         480
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         483
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         484
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   841 AA;  87638 MW;  04DF21EEEFF200B7 CRC64;
     MRVPLSWLAE YVDLAPGSTT EDVHAALVKV GLEEEDIHTF DVSGPVVVGE VLEFVEEPQS
     NGKTIRWCQV RVAPDGETAA DGGPAVHGIV CGADNFFVGD KVVVTLPGAV LPGPFPIAAR
     KTYGHVSDGM IASTRELGLG DEHDGILRLS TLGVDAEVGT DAIALLGLDD AAIEINVTPD
     RGYAFSIRGV AREYSHATGA TFRDPATRPE LVTPVGDGYP VAIDDVAPIR GRQGASVFAT
     RVVRGVDATR PTPPWMVSRL KLAGIRSISL LVDITNYVML ELGQPIHGYD LDHLTGGIVV
     RRAIGGETLE TLDGQKRKLD LEDLLITDGS GAIGLAGVMG GARTEMSDAT TNVLIEAANF
     DPVSIARTAR RHKLPSEASR RFERGVDPRI AVASAARVAE LMVSLAGGTT DAVAGVVGEP
     AEPEAIRFPG GYVSALIGVD YTDDEIRGSL EEIGATVADA DGGLLVTPPS WRPDLTDKSD
     LAEEVARIVG YDRIPSVLPV APAGRGLTRS QRIRRTVADT LAAAGSTEIL AFPFLGAEDN
     NLYGSPDSET VPAIKVANAL DASAPYLRTT LLPGLIAAAK HNLSRGLTDL SLFEVGLVFT
     PEAGRSYGQA ELPSGVALPT DEQLAELNDG IPPQPRHVGV LILGNAVPKQ PGQPAVASGI
     ADALAAVTQI GLATGAPIEV KQGSHKAMHP GRTAELWIGD RSIGFAGELL PQLALDSDLP
     RVVAVLELDL DALLESTDAA FTAGVIGTLP AATQDLSLVV SVDAPAAAVG AAVREGAGSL
     LEDIRLVDDY RGQGLADGTK SLTFALRFRA PDRTLTAAEA TEAKLAGSAL AAERFGAHIR
     D
//
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