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Database: UniProt
Entry: A0A0H3J9G4_CLOPA
LinkDB: A0A0H3J9G4_CLOPA
Original site: A0A0H3J9G4_CLOPA 
ID   A0A0H3J9G4_CLOPA        Unreviewed;       339 AA.
AC   A0A0H3J9G4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 24.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE            EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00281};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE            Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00281};
GN   Name=pheS {ECO:0000256|HAMAP-Rule:MF_00281,
GN   ECO:0000313|EMBL:AJA51738.1};
GN   ORFNames=CLPA_c16800 {ECO:0000313|EMBL:AJA51738.1};
OS   Clostridium pasteurianum DSM 525 = ATCC 6013.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA51738.1, ECO:0000313|Proteomes:UP000030905};
RN   [1] {ECO:0000313|EMBL:AJA51738.1, ECO:0000313|Proteomes:UP000030905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 525 / ATCC 6013 {ECO:0000313|Proteomes:UP000030905};
RX   PubMed=25700415;
RA   Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.;
RT   "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing
RT   Clostridium pasteurianum DSM 525.";
RL   Genome Announc. 3:e01591-14(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate +
CC         H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413,
CC         Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215;
CC         EC=6.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00281,
CC         ECO:0000256|SAAS:SAAS01124652};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00281};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00281};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS01133340}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00281,
CC       ECO:0000256|SAAS:SAAS00089481}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS00541523}.
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DR   EMBL; CP009268; AJA51738.1; -; Genomic_DNA.
DR   RefSeq; WP_003443620.1; NZ_JPGY02000001.1.
DR   STRING; 1262449.CP6013_3808; -.
DR   EnsemblBacteria; AJA51738; AJA51738; CLPA_c16800.
DR   EnsemblBacteria; KRU12254; KRU12254; CP6013_01501.
DR   KEGG; cpae:CPAST_c16800; -.
DR   KEGG; cpat:CLPA_c16800; -.
DR   PATRIC; fig|1262449.3.peg.1515; -.
DR   KO; K01889; -.
DR   OrthoDB; 469058at2; -.
DR   BioCyc; GCF_001856645:G1FB7-1653-MONOMER; -.
DR   Proteomes; UP000030905; 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:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR004188; Phe-tRNA_ligase_II_N.
DR   InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   TIGRFAMs; TIGR00468; pheS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110915};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110882};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030905};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00461853};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110936, ECO:0000313|EMBL:AJA51738.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00017000};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS00017079};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110884};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00281,
KW   ECO:0000256|SAAS:SAAS01110938};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030905}.
FT   METAL       254    254       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00281}.
SQ   SEQUENCE   339 AA;  38396 MW;  1711188F2BA5CD81 CRC64;
     MKEKLEDIKK SAIAELKSSV SKEEIEKLRV KYLGKKGELT QILRGMGTLS KEERPVIGKI
     ANEVRETIEG IINTSMDSIK KKEKEEKLKS EVIDISLPGK KQTIGHRNPL DITLRKTEEI
     FRSMGFTVEE GPEVEYDKYN FEMLNIPKGH PARGEQDTFY INDNIVLRTQ TSPVQIRTML
     NQKPPIKMIS PGKVYRSDAA DATHSPIFYQ VEGLVVDKGI TFADMKGTLE MYIKKMFGEN
     VKTKFRPHHF PFTEPSAELD ISCFACGGEG CKVCKGEGFI EMYGCGMVHP QVLRNCGIDP
     EVYSGFAFGV GLDRIVMQTL GIDDIRQLYE SDMRFLDQF
//
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