ID I6DEJ8_SHIBO Unreviewed; 795 AA. AC I6DEJ8; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 27-SEP-2017, entry version 38. 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 ECO:0000313|EMBL:EIQ30190.1}; GN ORFNames=SB96558_2311 {ECO:0000313|EMBL:EIQ30190.1}; OS Shigella boydii 965-58. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766138 {ECO:0000313|EMBL:EIQ30190.1, ECO:0000313|Proteomes:UP000004209}; RN [1] {ECO:0000313|EMBL:EIQ30190.1, ECO:0000313|Proteomes:UP000004209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=965-58 {ECO:0000313|EMBL:EIQ30190.1, RC ECO:0000313|Proteomes:UP000004209}; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). {ECO:0000256|HAMAP- CC Rule:MF_00283, ECO:0000256|SAAS:SAAS00385044}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC 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|HAMAP-Rule:MF_00283, ECO:0000256|SAAS:SAAS00385214}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283, CC ECO:0000256|SAAS:SAAS00710994}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta CC subunit family. Type 1 subfamily. {ECO:0000256|HAMAP- CC Rule:MF_00283, ECO:0000256|SAAS:SAAS00570605}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIQ30190.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AKNA01000053; EIQ30190.1; -; Genomic_DNA. DR ProteinModelPortal; I6DEJ8; -. DR EnsemblBacteria; EIQ30190; EIQ30190; SB96558_2311. DR PATRIC; fig|766138.3.peg.2360; -. DR Proteomes; UP000004209; 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; cd02796; tRNA_bind_bactPheRS; 1. DR Gene3D; 3.30.70.380; -; 1. DR Gene3D; 3.50.40.10; -; 1. DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1. DR InterPro; IPR005146; B3/B4_tRNA-bd. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR005121; Fdx_antiC-bd. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu. DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR033714; tRNA_bind_bactPheRS. DR InterPro; IPR005147; tRNA_synthase_B5-dom. DR Pfam; PF03483; B3_4; 1. DR Pfam; PF03484; B5; 1. DR Pfam; PF03147; FDX-ACB; 1. DR Pfam; PF01588; tRNA_bind; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SMART; SM00896; FDX-ACB; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54991; SSF54991; 1. DR SUPFAM; SSF56037; SSF56037; 1. DR TIGRFAMs; TIGR00472; pheT_bact; 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|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00089714, ECO:0000313|EMBL:EIQ30190.1}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00089645}; KW Complete proteome {ECO:0000313|Proteomes:UP000004209}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00710959}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00089691, ECO:0000313|EMBL:EIQ30190.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00089695}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00089707}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00462081}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00283, KW ECO:0000256|SAAS:SAAS00089659}; KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00209, KW ECO:0000256|SAAS:SAAS00514389}; KW tRNA-binding {ECO:0000256|PROSITE-ProRule:PRU00209, KW ECO:0000256|SAAS:SAAS00514462}. FT DOMAIN 39 148 TRNA-binding. {ECO:0000259|PROSITE: FT PS50886}. FT DOMAIN 401 476 B5. {ECO:0000259|PROSITE:PS51483}. FT DOMAIN 701 794 FDX-ACB. {ECO:0000259|PROSITE:PS51447}. FT METAL 454 454 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00283}. FT METAL 460 460 Magnesium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00283}. FT METAL 463 463 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00283}. FT METAL 464 464 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00283}. SQ SEQUENCE 795 AA; 87308 MW; 41BE2F5672D92A69 CRC64; MKFSELWLRE WVNPAIDSDA LANQITMAGL EVDGVEPVAG SFHGVVVGEV VECAQHPNAD KLRVTKVNVG GDRLLDIVCG APNCRQGLRV AVATIGAVLP GDFKIKAAKL RGEPSEGMLC SFSELGISDD HSGIIELPAD APIGTDIREY LKLDDNTIEI SVTPNRADCL GIIGVARDVA VLNQLPLVEP EIVPVGATID DTLPITVEAP EACPRYLGRV VKGINVKAPT PLWMKEKLRR CGIRSIDAVV DVTNYVLLEL GQPMHAFDKD RIEGGIVVRM AKEGETLVLL DGTEAKLNAD TLVIADHNKA LAMGGIFGGE HSGVNDETQN VLLECAFFSP LSITGRARRH GLHTDASHRY ERGVDPALQH KAMERATRLL IDICGGEAGP VIDITSEATL PKRATITLRR SKLDRLIGHH IADEQVTDIL RRLGCEVTEG KDEWQAVAPS WRFDMEIEED LVEEVARVYG YNNIPDEPVQ ASLIMGTHRE ADLSLKRVKT LLNDKGYQEV ITYSFVDPKV QQMIHPGVEA LLLPSPISVE MSAMRLSLWT GLLATVVYNQ NRQQNRVRIF ESGLRFVPDT QAPLGIRQDL MLAGVICGNR YEEHWNLAKE TVDFYDLKGA LESVLDLTGK LNEVEFRAEA NPALHPGQSA AIYLKGERIG FVGVVHPELE RKLDLNGRTL VFELEWNKLA DRVVPQAREI SRFPANRRDI AVVVAENVPA ADILSECKKV GVNQVVGVNL FDVYRGKGVA EGYKSLAISL ILQDTSRTLE EEEIAATVAK CVEALKERFQ ASLRD //