ID   SYA_LEUCK               Reviewed;         894 AA.
AC   B1MXP8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=LCK_00467;
OS   Leuconostoc citreum (strain KM20).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=349519;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM20;
RX   PubMed=18281406; DOI=10.1128/jb.01862-07;
RA   Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA   Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT   "Complete genome sequence of Leuconostoc citreum KM20.";
RL   J. Bacteriol. 190:3093-3094(2008).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC       editing domain and the C-terminal C-Ala domain. The editing domain
CC       removes incorrectly charged amino acids, while the C-Ala domain, along
CC       with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC       editing and aminoacylation centers thus stimulating deacylation of
CC       misacylated tRNAs (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ489736; ACA82300.1; -; Genomic_DNA.
DR   RefSeq; WP_004908976.1; NC_010471.1.
DR   AlphaFoldDB; B1MXP8; -.
DR   SMR; B1MXP8; -.
DR   STRING; 349519.LCK_00467; -.
DR   EnsemblBacteria; ACA82300; ACA82300; LCK_00467.
DR   KEGG; lci:LCK_00467; -.
DR   eggNOG; COG0013; Bacteria.
DR   HOGENOM; CLU_004485_1_1_9; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 91428at2; -.
DR   Proteomes; UP000002166; 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: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; IPR003156; DHHA1_dom.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF02272; DHHA1; 1.
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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding.
FT   CHAIN           1..894
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000347660"
SQ   SEQUENCE   894 AA;  97806 MW;  7188A165A6397D7E CRC64;
     MKELTSSEVR QMFLDFFASK GHEIVPSKNL IPQDDPTLLW INSGVATLKK YFDGSVIPKN
     PRITNAQKAI RTNDIENVGK TARHHTLFEM MGNFSVGDYF KAEVIPWAWE LLTSPEWYGL
     DKDLLYVTVY PKDQEAKKIW LEKTDLPEGH IYEVEDNFWD IGEGPSGPDS EIFFDRGPAF
     QNLPDNDPEM YPGGENERYL EIWNIVFSQF NHLPGLTDNA QYPELPHKNI DTGMGLERLV
     SVFQNGRTNF DTDLFLPIIR ATEKMSPDYT YDATKDSESN TSFKVIADHI RAITFAIGDG
     ALPANEGRGY VIRRLLRRAV LHGQKLGIQG EFLTKLVPIV AEIMQSYYPE IADNTEKIQK
     TIAAEEKRFN ATLTGGLSLL NDVIAKAKAS GQQVISGADA FKLSDTYGFP LELTQEQAAD
     EGLTVDVVGF NDALQAQRTR ARAARSNDKS MGVQNAVLTD LKVPSDYVGW SETEVSNAAI
     VAIIGHDNQG VDALLANAEP GDSVQLVFDK TPFYAEMGGQ VADQGEVLNK QGEVVARVTD
     TQSAPNGQHV HTVEVVTSFK LGDQVALKVN LARHVAISKN HTATHLLDQT LRNVIGGDVH
     QAGSLVEPEY LRFDFTHEGP VSEQNLEKIE TMVNQVIANN LPITWVETDI ESAKKMGAVA
     VFGEKYGDVV RVVSIGDFNK EFDGGTHAQT TAELGLFKIV SESGIGAGVR RIEAVTGLAA
     LSQFKAEEQA LKVIADSLKA QKLTDAPAKV EDLQVEIKTL QRHLTSVEAQ LANAAAQDVF
     KDVKTQNGYQ YITAQLQVSG MDGLRQVVDT WRENYPSDVL VLATHVDDKV SLIVAASPEA
     NKKGFKAGDL IKAIAPKIGG GGGGRPDMAQ AGGKNPAGIN DAFSAVSTFL DELA