ID   A0A059ZTE3_ACIBA        Unreviewed;       878 AA.
AC   A0A059ZTE3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   08-JUN-2016, entry version 22.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00015689};
DE            EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00015673};
DE   AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036};
GN   Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036};
GN   ORFNames=ACX60_12345 {ECO:0000313|EMBL:AKQ27505.1}, APB90_01250
GN   {ECO:0000313|EMBL:KQE73876.1}, AZE33_07035
GN   {ECO:0000313|EMBL:AMN00940.1}, TE32_12855
GN   {ECO:0000313|EMBL:AKJ46435.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:KQE73876.1, ECO:0000313|Proteomes:UP000051044};
RN   [1] {ECO:0000313|EMBL:AKQ27505.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 17978-mff {ECO:0000313|EMBL:AKQ27505.1};
RX   PubMed=26170289; DOI=10.1073/pnas.1502966112;
RA   Weber B.S., Ly P.M., Irwin J.N., Pukatzki S., Feldman M.F.;
RT   "A multidrug resistance plasmid contains the molecular switch for type
RT   VI secretion in Acinetobacter baumannii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:9442-9447(2015).
RN   [2] {ECO:0000313|EMBL:AKJ46435.1, ECO:0000313|Proteomes:UP000035522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH386 {ECO:0000313|EMBL:AKJ46435.1,
RC   ECO:0000313|Proteomes:UP000035522};
RA   Fang Y., Hua X., Feng Y., Lil X., Weng J., Ruan Z., Shang S., Yu Y.;
RT   "Complete genome sequence of a multi-drug resistant ST208
RT   Acinetobacter baumannii.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000036024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978-mff {ECO:0000313|Proteomes:UP000036024};
RA   Weber B.S., Ly P.M., Irwin J.N., Pukatzki S., Feldman M.F.;
RT   "A multidrug resistance plasmid contains the molecular switch for type
RT   VI secretion in Acinetobacter baumannii.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:KQE73876.1, ECO:0000313|Proteomes:UP000051044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABBL094 {ECO:0000313|EMBL:KQE73876.1,
RC   ECO:0000313|Proteomes:UP000051044};
RA   Ozer E.A., Fitzpatrick M.A., Hauser A.R.;
RT   "The utility of whole genome sequencing in characterizing
RT   Acinetobacter epidemiology and analyzing hospital outbreaks.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:AMN00940.1, ECO:0000313|Proteomes:UP000070590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH858 {ECO:0000313|EMBL:AMN00940.1,
RC   ECO:0000313|Proteomes:UP000070590};
RA   Feng Y., Hua X., Yu Y.;
RT   "Complete genome of Acinetobacter baumannii str. XH858.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a
CC       two-step reaction: alanine is first activated by ATP to form Ala-
CC       AMP and then transferred to the acceptor end of tRNA(Ala). Also
CC       edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its
CC       editing domain. {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00345671}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP +
CC       diphosphate + L-alanyl-tRNA(Ala). {ECO:0000256|HAMAP-
CC       Rule:MF_00036, ECO:0000256|SAAS:SAAS00015802}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00036};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00015710}.
CC   -!- DOMAIN: Consists of three domains; the N-terminal catalytic
CC       domain, the editing domain and the C-terminal C-Ala domain. The
CC       editing domain removes incorrectly charged amino acids, while the
CC       C-Ala domain, along with tRNA(Ala), serves as a bridge to
CC       cooperatively bring together the editing and aminoacylation
CC       centers thus stimulating deacylation of misacylated tRNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00541271}.
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DR   EMBL; CP010779; AKJ46435.1; -; Genomic_DNA.
DR   EMBL; CP012004; AKQ27505.1; -; Genomic_DNA.
DR   EMBL; CP014528; AMN00940.1; -; Genomic_DNA.
DR   EMBL; LLGV01000351; KQE73876.1; -; Genomic_DNA.
DR   RefSeq; WP_000199457.1; NZ_LRMK01000036.1.
DR   EnsemblBacteria; AKJ46435; AKJ46435; TE32_12855.
DR   EnsemblBacteria; AKQ27505; AKQ27505; ACX60_12345.
DR   EnsemblBacteria; KGF59377; KGF59377; LH92_05680.
DR   EnsemblBacteria; KHT72979; KHT72979; RW53_10290.
DR   EnsemblBacteria; KHT87263; KHT87263; RW49_09885.
DR   EnsemblBacteria; KHV12554; KHV12554; RW59_15070.
DR   EnsemblBacteria; KHV19248; KHV19248; RW56_13355.
DR   EnsemblBacteria; KHV24895; KHV24895; RW57_13055.
DR   EnsemblBacteria; KHV29702; KHV29702; RW60_15450.
DR   EnsemblBacteria; KHV34627; KHV34627; RW58_10455.
DR   EnsemblBacteria; KHX50032; KHX50032; RQ85_07295.
DR   EnsemblBacteria; KHY02703; KHY02703; RQ47_12925.
DR   EnsemblBacteria; KJE57151; KJE57151; RQ42_17590.
DR   EnsemblBacteria; KJE57186; KJE57186; RQ37_17560.
DR   EnsemblBacteria; KJE65061; KJE65061; RR20_14500.
DR   EnsemblBacteria; KJE69651; KJE69651; RQ98_13555.
DR   EnsemblBacteria; KJE70549; KJE70549; RR27_13600.
DR   EnsemblBacteria; KJF09521; KJF09521; RQ64_14245.
DR   EnsemblBacteria; KJF11490; KJF11490; RQ49_13880.
DR   EnsemblBacteria; KJG74254; KJG74254; RQ82_10760.
DR   EnsemblBacteria; KKZ42688; KKZ42688; UN98_00130.
DR   EnsemblBacteria; KOP84734; KOP84734; AKG97_17310.
DR   EnsemblBacteria; KPA47230; KPA47230; AC795_18790.
DR   KEGG; abaa:IX88_07955; -.
DR   KEGG; abw:BL01_15570; -.
DR   eggNOG; ENOG4105CIM; Bacteria.
DR   eggNOG; COG0013; LUCA.
DR   KO; K01872; -.
DR   Proteomes; UP000035522; Chromosome.
DR   Proteomes; UP000036024; Chromosome.
DR   Proteomes; UP000051044; Unassembled WGS sequence.
DR   Proteomes; UP000070590; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
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.
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   TIGRFAMs; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423727, ECO:0000313|EMBL:AKJ46435.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423789}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035522,
KW   ECO:0000313|Proteomes:UP000036024, ECO:0000313|Proteomes:UP000051044,
KW   ECO:0000313|Proteomes:UP000070590};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423773};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423735, ECO:0000313|EMBL:KQE73876.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423853};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423841};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423730};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423770};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423767};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00423813}.
FT   DOMAIN        1    713       AA_TRNA_LIGASE_II_ALA.
FT                                {ECO:0000259|PROSITE:PS50860}.
FT   COILED      736    763       {ECO:0000256|SAM:Coils}.
FT   METAL       562    562       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       566    566       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       670    670       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       674    674       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
SQ   SEQUENCE   878 AA;  96528 MW;  48DC937CBAF0C6F6 CRC64;
     MTSAEIREAF LRYFETQGHT RVASSSLVPA NDPTLLFTNA GMNQFKDCFL GLEKRDYVRA
     TTSQKCVRAG GKHNDLDNVG YTARHHTFFE MLGNFSFGDY FKRDALKFAW EFLTSEQWLA
     LPKDKLYVTV YHTDDEAYDI WNKEIGLAPE RIIRIGDNKG EKYASDNFWA MGDTGPCGPC
     SEIFFDHGEH IWGGLPGSPE EDGDRFIEIW NNVFMQFNRT ADGVLHPLPA PSVDTGMGLE
     RISAVLQHVN SNYDIDLFQH LLKAAANIIG IEDEGQPSLR VVADHARSCC FLIADGVNPS
     NEGRGYVLRR IIRRAVRHGN KLGATGTFFY KMLQPLIEVM GQAYPELEAR REVIEATLIR
     EEEQFAKTLE QGLKLLEGEL AQLKDKTIPG ATVFKLYDTY GFPTDLTADI ARERGFIIDE
     AGFEVEMAAQ RQRARDAGKF AVDYNNIVKV EGETQFDGYT NTTGQGQIVA IYKDGVQVDE
     VSEGDEALIV LNQTPFYAES GGQIGDTGIF KNETGIFEVQ DTKKSGGAFV HQGIVTVGNL
     KTSQNVEAIV KADIREATAR NHSATHLLHA ALRQILGSHV QQKGSLVASD ILRFDFANDQ
     PVSFEQLQQV ERLVNAEIIA NTAVTTELLD IETAKAKGAM MLFGEKYGDE VRVLSMGSVI
     DEKNFSIELC GGIHVKRTGD IGLFKITSEG GVAAGVRRIE AVTGTKALEV VQKADHDIQH
     INSLLKAQKD QTVERVQANV ELVSALQKQI EQLNQKLANF QAADLIDQVQ TIAGRQTLIT
     TVQGVDAKAL RNLHDSVKSK LENAVIVLAG VEGDKVSLLA SVASQYTANL KAGDIIKHLA
     TELGGKGGGK PDLAQGGAPL NEKFGQVMAA LPAWLEQK
//