SYA_LACPL
ID SYA_LACPL Reviewed; 880 AA.
AC Q88V10; F9UQJ6;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=lp_2277;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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}.
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; AL935263; CCC79485.1; -; Genomic_DNA.
DR RefSeq; WP_011101703.1; NC_004567.2.
DR RefSeq; YP_004889999.1; NC_004567.2.
DR AlphaFoldDB; Q88V10; -.
DR SMR; Q88V10; -.
DR STRING; 220668.lp_2277; -.
DR EnsemblBacteria; CCC79485; CCC79485; lp_2277.
DR KEGG; lpl:lp_2277; -.
DR PATRIC; fig|220668.9.peg.1927; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_9; -.
DR OMA; YHHTMFE; -.
DR PhylomeDB; Q88V10; -.
DR BioCyc; LPLA220668:G1GW0-1969-MON; -.
DR Proteomes; UP000000432; 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; Reference proteome; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..880
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075130"
SQ SEQUENCE 880 AA; 97266 MW; BB5217FEA3988508 CRC64;
MKKLSSSEIR QMYLDFFHEK GHTIVPSASL VPVDDPTLLW INSGVATMKK YFDGSVVPDN
PRMTSSQKSI RTNDIENVGR TARHHTLFEM LGNFSVGDYF KKEAISWAWE LLTSPKWFGW
DPDKLYMTVY PKDTDAAKFW EATGVKPDHI IKVEDNFWDI GQGPSGPDSE IFYDRGEAFN
NLADDDPENY PGGENERYLE VWNIVFSQFN HTPEGTYEPL PRKNIDTGMG LERVVSVFQN
AKTNFETDLF LPIIHKTEEL SDGKHYGDNA QDDVSFKVIA DHARAITFAI SDGALPSNEG
RGYVIRRLIR RAILHGQKLG LKEAFLDQLV PIVGKIMASH YPDVLKNSAY IEKIVASEES
RFNETLNDGL NLLNNLIAET KQTGHDTLAG KDAFKLYDTY GFPFELTKEY AGDEDLDVDE
AGFEVEMKAQ RDRARNARSS AKSMGVQRSL LIDIKTPSEY VGYDELTNVQ GTLNDIIVDE
TLVDHVDSGQ AEMIFSKTPF YAEMGGQVAD RGVILDDAGE MVAKVTDVQN APNKQHLHTV
EVLKPMRKDA TYTLNVDLAF HNKVEKNHTA THLLDQALRD VLGEHTKQAG SLVEPDYLRF
DFTHFGQVTD EELAKVEQIV NDKIWAALPV SAIQTDQETG HKMGAIAVFT EKYGKIVRVV
SIGDYSIEFD GGTHVKNSSE LGLFKIVSET GIGAGTRRIE AVTSKEAFEL LAGEEQTLKQ
VAAQVKAPKL ADTPAKVSQL QADLKAEQQN RASLESRLAK QQAGAVFDQV DDVNGTTLIA
QQIEVSGMDQ LRQLADTWKT KQYSDVLVLG TVIGEKVNLL VAVSDDKVKA GIKAGDLIKA
IAPKVGGGGG GRPTLAQAGG KKPAGLPVAL KAAHEWLAEQ
