ID A0A0K2G731_NITMO Unreviewed; 571 AA.
AC A0A0K2G731;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN Name=pheT {ECO:0000313|EMBL:ALA56763.1};
GN ORFNames=NITMOv2_0325 {ECO:0000313|EMBL:ALA56763.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA56763.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA56763.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA56763.1,
RC ECO:0000313|Proteomes:UP000069205};
RX PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA Nielsen P.H., Wagner M., Daims H.;
RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT from the genus Nitrospira.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000256|ARBA:ARBA00007438}.
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DR EMBL; CP011801; ALA56763.1; -; Genomic_DNA.
DR RefSeq; WP_053378202.1; NZ_CP011801.1.
DR AlphaFoldDB; A0A0K2G731; -.
DR STRING; 42253.NITMOv2_0325; -.
DR KEGG; nmv:NITMOv2_0325; -.
DR PATRIC; fig|42253.5.peg.313; -.
DR OrthoDB; 9805455at2; -.
DR Proteomes; UP000069205; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00769; PheRS_beta_core; 1.
DR Gene3D; 3.30.56.10; -; 2.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 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; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR NCBIfam; TIGR00471; pheT_arch; 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; PF03484; B5; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR PROSITE; PS51483; B5; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:ALA56763.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ALA56763.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000069205}.
FT DOMAIN 288..363
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 571 AA; 63164 MW; CDA51F1B9741DC90 CRC64;
MPTISIFKDD FEALLGGKAK GVVSIEQLEE WLTLVKGELK GHNPETGELR VELQDSNRPD
LWCCEGIARQ IRIKQQGKLK PYAFFGNKRK SHQRLIVGQG LEEVRPYVAA CMAKGYRVTD
QGLAQLIQTQ EKLADIFGHK RKTVSIGIYQ LPKIVFPVVY ELVKPDEARF TPLGMETVMT
LSEILMVHPK GLEHGHILAG QKLVPFLRDA QHQPLSFPPI INSREIGEVR VGDEELFVEV
TGTDLSMVML TLNIFAANLA DRGADVEPIE VQYPRTTPLG KRVVAPRDLG RPRTIDITTI
ERALGQELGA KTVKQALEVY GYDVSIGRGT VKAKLPPYRQ DLMHAMDVVE DVAISRGYGS
FLPVMPAQFT VGGLSRIEQT SDRARELMVG MGFQEIISNI LGSPENYCSA MRLDGTEWGR
MVEVDNAMAA TFSCLRQWML PSLLRVEAAS SRAFYPHRLF EAGEVAIPDG FHELGSRSET
VLGAVIAHAS AHFSEIHSCL DVLCYHLGKE YGLEPVQHPS FLEGRAGRIV VGGQSLGVIG
EVHPEVLERW QIAVPVVSFD LNLTQLIEAG G
//
