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Database: UniProt
Entry: F9ZFC8_9PROT
LinkDB: F9ZFC8_9PROT
Original site: F9ZFC8_9PROT 
ID   F9ZFC8_9PROT            Unreviewed;       790 AA.
AC   F9ZFC8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 74.
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=NAL212_2128 {ECO:0000313|EMBL:ADZ26960.1};
OS   Nitrosomonas sp. AL212.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ26960.1, ECO:0000313|Proteomes:UP000001629};
RN   [1] {ECO:0000313|EMBL:ADZ26960.1, ECO:0000313|Proteomes:UP000001629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL212 {ECO:0000313|EMBL:ADZ26960.1,
RC   ECO:0000313|Proteomes:UP000001629};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y., Klotz M.G.,
RA   Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.;
RT   "Complete sequence of chromosome of Nitrosomonas sp. AL212.";
RL   Submitted (FEB-2011) 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; CP002552; ADZ26960.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9ZFC8; -.
DR   STRING; 153948.NAL212_2128; -.
DR   KEGG; nit:NAL212_2128; -.
DR   eggNOG; COG0072; Bacteria.
DR   HOGENOM; CLU_016891_0_0_4; -.
DR   Proteomes; UP000001629; Chromosome.
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:UP000001629};
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..149
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
FT   DOMAIN          402..477
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
FT   DOMAIN          696..789
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51447"
FT   BINDING         455
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         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         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"
FT   BINDING         465
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   790 AA;  88560 MW;  FF823F0320115726 CRC64;
     MKFSEIWLRS FVNPACSGDQ LAHALTMAGI EVESIEPVAS DFDNVIVAEV VSVERHPTAD
     RLYVCNVKTG KSDNDLLQIV CGAPNVSAGV RVPCALIGAN LPNLMIRKTK LRGIDSSGML
     CSGKELGISE VAEGLLLLPN DAPVGMDFRS YYQLEDRVFT LSLTPNRADC LSVQGVAREV
     SAITDTDIQL PFAIENVSDE INDTLNVYVI APDACPLYCG RLLRNINLNV STPLWLTQRL
     ERSGIRSINP VVDITNYVML EIGQPMHAFD LTKITGGSIQ VRYAFSHEKI QLLNGDQVDL
     TPEMLLITDE HKPLALAGIM GGLESGVTYG TTDIFLESAF FNPTVISGKS FHLGFSSDSA
     YRFERGVDFE TTRNALERAS YLIHSICGGQ TGTVIEIKNE LPQRSSVDVR MERIKRILGI
     DLNREQIGNY FRRLGFKFSE KDKCFSVIPP TYRFDLMIEE DFVEELARIY GYDHIPTYYP
     YASMAMVPAP ETQHTTTEIK QTLINLDYQE VINYSFVDAG WEADLVDNHK PITLLNPISN
     QMNVMRSTLI GGLIANLQFN LNRKQVRVRL FEVGCCFLRE DVSDCKQIEK ISGLSYGDFS
     SEQWGIAARN VDFYDVKADV EVLCRGKSVE FKRFSHPALH PGKSAEIYFE DRIIGWIGEL
     HPRWQTKYSL QKNTILFELD LHSLKPRPLP LIKEISKFPP VRRDIAIIVD NDISAYSLLS
     SMQAVKSTII SDISLFDIYR GNGMESNKKS LAFRVLLQDT EKTLTDEQVE SAVTSLISIL
     KNQFGAELRN
//
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