SYA_STRPS
ID SYA_STRPS Reviewed; 872 AA.
AC B2IQK0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00036};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_00036};
GN Name=alaS {ECO:0000255|HAMAP-Rule:MF_00036}; OrderedLocusNames=SPCG_1372;
OS Streptococcus pneumoniae (strain CGSP14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=516950;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGSP14;
RX PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT "Genome evolution driven by host adaptations results in a more virulent and
RT antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL BMC Genomics 10:158-158(2009).
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. {ECO:0000255|HAMAP-Rule:MF_00036}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}.
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. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00036}.
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DR EMBL; CP001033; ACB90624.1; -; Genomic_DNA.
DR RefSeq; WP_000811756.1; NC_010582.1.
DR AlphaFoldDB; B2IQK0; -.
DR SMR; B2IQK0; -.
DR EnsemblBacteria; ACB90624; ACB90624; SPCG_1372.
DR KEGG; spw:SPCG_1372; -.
DR HOGENOM; CLU_004485_1_1_9; -.
DR OMA; YHHTMFE; -.
DR Proteomes; UP000001682; 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; 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; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..872
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347819"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 673
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 872 AA; 96441 MW; 8D14A87012CFD097 CRC64;
MKQLSSAQVR QMWLDFWATK GHSVEPSVSL VPVNDPTLLW INSGVATLKK YFDGTIIPEN
PRITNAQKAI RTNDIENVGK TARHHTMFEM LGNFSIGDYF RDEAITWAYE LLTSPEWFDF
PAEKLYMTYY PDDKDSYNRW IEVGVDPSHL IPIEDNFWEI GAGPSGPDTE IFFDRGEAFD
PENIGLRLLA EDIENDRYIE IWNIVLSQFN ADPAVPRSEY KELPHKNIDT GAGLERLVAV
IQGAKTNFET DLFMPIIREV EKLSGKVYDQ DGDNMSFKVI ADHIRSLSFA IGDGALPGNE
GRGYVLRRLL RRASMHGQKL GINEPFLYKL VPTVGKIMES YYPEVLEKRD FIEKIVKSEE
ESFARTLHSG QHFAQGIVAD LKEKGQSVIA GQDVFKLYDT YGFPVELTEE IAEEAGMTVD
REGFEAAMKE QQERARASAV KGGSMGMQNE TLQNITVESV FNYNTSQLSS KLVAIVADNA
EVGAVSEGTA SLIFAETSFY AEMGGQVADY GQILDESGKI VATVTNVQKA PNGQALHTVE
VLAPLALNQE YTLAIDSNRR HRVMKNHTAT HLLHAALHNI LGNHATQAGS LNEVEFLRFD
FTHFQAVTAE ELRAIEQQVN EKIWEALEVK TVETDIDTAK EMGAMALFGE KYGKEVRVVT
IGDYSIELCG GTHVGNTSEI GLFKIVKEEG IGSGTRRILA VTGKEAFEAY REQEDALKAI
AATLKAPQVK EVPHKVEGLQ EQLRQLQKEN AELKEKAAAA AAGDIFKDVK EVNGHRYIAS
QVSVSDAGAL RTFADNWKQK DYSDLLVLVA AIGDKVNVLV ASKTKDLHAG NLVKELAPII
DGRGGGKPDM AMAGGSNQAK IQELLDAVAG KL
