ID   SYA_BORGP               Reviewed;         594 AA.
AC   Q662E4;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Alanine--tRNA ligase;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
GN   Name=alaS; OrderedLocusNames=BG0223;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(2004).
CC   -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC       step reaction: alanine is first activated by ATP to form Ala-AMP and
CC       then transferred to the acceptor end of tRNA(Ala). Also edits
CC       incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC       domain (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC         tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC         COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Consists of two domains; the N-terminal catalytic domain (in
CC       this organism this is shorter than usual) and the editing domain; the
CC       C-terminal C-Ala domain found in most orthologs is missing. The editing
CC       domain removes incorrectly charged amino acids (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000013; AAU07077.1; -; Genomic_DNA.
DR   RefSeq; WP_011193565.1; NZ_CP028872.1.
DR   AlphaFoldDB; Q662E4; -.
DR   SMR; Q662E4; -.
DR   STRING; 290434.BG0223; -.
DR   PRIDE; Q662E4; -.
DR   EnsemblBacteria; AAU07077; AAU07077; BG0223.
DR   KEGG; bga:BG0223; -.
DR   eggNOG; COG0013; Bacteria.
DR   HOGENOM; CLU_004485_0_2_12; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 91428at2; -.
DR   Proteomes; UP000002276; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR   InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF101353; SSF101353; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT   CHAIN           1..594
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000075073"
FT   BINDING         456
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         460
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         558
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         562
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   594 AA;  67664 MW;  C0ACE947C796332D CRC64;
     MTLDKLRKKY IDFFKSKKHF EIMGKSLVPE NDPTVLFNTA GMQPLIPYLL GEVHPSGDML
     VNVQKCLRTG DIDEVGDLSH LTFFEMLGNW SLGAYFKEYS VKCSFEFLTS SDYLNIPKDS
     LYVSVFEGDQ KIPCDTETAK VWESLGIPKD RIYYLSKAHN FWGPVGSKGP CGPDTEIYVD
     TGKIKCSLDC NITCSCGKYF EIWNNVFMQY NKDENGNYIE LDRKCVDTGM GLERTIAFLQ
     GKSSVYDTDA FIPIIKRIEV ISGKIYGQKE DDDRCIRIIS DHVKAACFIL ADSSVVSPSN
     LGQGYVLRRL IRRSIRYAKK LGIKSHFLAD LVDSIETIYG SFYNELTEKK DFIKKELSTE
     EEKFFKTLFQ GEQEFIKITR NLPSKTIPGD IAFKLYDTYG FPYEVTEELA FEYGFNIDKV
     GFDEYFKKHQ KTSKKGGDKV FKGGLADYTY ETTRLHTATH LLHKALQLVL GDHVRQKGSN
     ITAERLRFDF VHSEKMTDDE IKKVEEIVNL QIKNSLSVKK SIMELSEAQK KGAMALFGEK
     YDNLVSVYEI DGFSLEVCGG PHVENTNELG TFKIQKEQSS SSGIRRIKAI LIDK