ID   A0A059ZTE3_ACIBA        Unreviewed;       878 AA.
AC   A0A059ZTE3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   26-FEB-2020, entry version 59.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036};
DE            EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036};
DE   AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036};
DE            Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_00036};
GN   Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036,
GN   ECO:0000313|EMBL:ASF76661.1};
GN   ORFNames=A7M79_15050 {ECO:0000313|EMBL:OIH04575.1}, A7M90_08745
GN   {ECO:0000313|EMBL:OIG67468.1}, B9X91_12675
GN   {ECO:0000313|EMBL:OTL19830.1}, B9X95_03515
GN   {ECO:0000313|EMBL:OTM92370.1}, BGC29_16755
GN   {ECO:0000313|EMBL:ODP71357.1}, C2U32_02220
GN   {ECO:0000313|EMBL:AUT36896.1}, CBI29_01280
GN   {ECO:0000313|EMBL:ASF76661.1}, DOL94_06455
GN   {ECO:0000313|EMBL:PZM17994.1}, E2533_01975
GN   {ECO:0000313|EMBL:TEX20686.1}, E2536_02285
GN   {ECO:0000313|EMBL:TEX31091.1}, FD913_18160
GN   {ECO:0000313|EMBL:TLT61917.1}, FJU79_12405
GN   {ECO:0000313|EMBL:TPS84755.1}, FJV14_14120
GN   {ECO:0000313|EMBL:TPS01309.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:PZM17994.1, ECO:0000313|Proteomes:UP000248662};
RN   [1] {ECO:0000313|EMBL:OIG67468.1, ECO:0000313|Proteomes:UP000179791, ECO:0000313|Proteomes:UP000179937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH639 {ECO:0000313|EMBL:OIH04575.1,
RC   ECO:0000313|Proteomes:UP000179791}, and XH647
RC   {ECO:0000313|EMBL:OIG67468.1, ECO:0000313|Proteomes:UP000179937};
RA   Hua X., Yu Y.;
RT   "The evolution of Acinetobacter baumannii in vivo.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ODP71357.1, ECO:0000313|Proteomes:UP000094982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH198 {ECO:0000313|EMBL:ODP71357.1,
RC   ECO:0000313|Proteomes:UP000094982};
RA   Mu X., Wang N., Li X., Shi K., Zhou Z., Yu Y., Hua X.;
RT   "The effect of colistin resistance-associated mutations on the fitness of
RT   Acinetobacter baumannii.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:OTL19830.1, ECO:0000313|Proteomes:UP000194699, ECO:0000313|Proteomes:UP000194957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR350 {ECO:0000313|EMBL:OTM92370.1,
RC   ECO:0000313|Proteomes:UP000194699}, and PR354
RC   {ECO:0000313|EMBL:OTL19830.1, ECO:0000313|Proteomes:UP000194957};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ASF76661.1, ECO:0000313|Proteomes:UP000197701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A85 {ECO:0000313|EMBL:ASF76661.1,
RC   ECO:0000313|Proteomes:UP000197701};
RA   Hamidian M., Wick R.R., Hawkey J., Holt K.E., Hall R.M.;
RT   "Complete genome sequence of Acinetobacter baumannii strain A85 belonging
RT   to global clone 1 (GC1).";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|Proteomes:UP000236385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABNIH28 {ECO:0000313|Proteomes:UP000236385};
RX   PubMed=29437920;
RG   NISC Comparative Sequencing Program;
RA   Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA   Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA   Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT   "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT   Bacterial Plasmids Conferring Carbapenem Resistance.";
RL   MBio 9:e02011-17(2018).
RN   [6] {ECO:0000313|EMBL:AUT36896.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT36896.1};
RG   NISC Comparative Sequencing Program;
RA   Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA   Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA   Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT   "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT   Bacterial Plasmids Conferring Carbapenem Resistance.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|Proteomes:UP000236385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABNIH28 {ECO:0000313|Proteomes:UP000236385};
RA   Segre J.A., Mullikin J.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:AUT36896.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT36896.1};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:PZM17994.1, ECO:0000313|Proteomes:UP000248662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R10 {ECO:0000313|EMBL:PZM17994.1,
RC   ECO:0000313|Proteomes:UP000248662};
RA   Bonnin R.A., Levy M., Cuzon G., Dortet L., Naas T.;
RT   "Carbapenemase-producing Acinetobacter spp. from environmental sources in
RT   an hospital from French Polynesia.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [10] {ECO:0000313|EMBL:TEX20686.1, ECO:0000313|Proteomes:UP000297480, ECO:0000313|Proteomes:UP000297782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDR-CQB {ECO:0000313|EMBL:TEX20686.1,
RC   ECO:0000313|Proteomes:UP000297782}, and MDR-CQE
RC   {ECO:0000313|EMBL:TEX31091.1, ECO:0000313|Proteomes:UP000297480};
RA   Jian Z.;
RT   "Resequencing Analysis and Multi-drug Resistance Differences of
RT   Acinetobacter baumannii in Chongqing, China.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [11] {ECO:0000313|EMBL:TLT61917.1, ECO:0000313|Proteomes:UP000309525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aci00849 {ECO:0000313|EMBL:TLT61917.1,
RC   ECO:0000313|Proteomes:UP000309525};
RA   Eigenbrod T., Reuter S., Gross A., Kocer K., Guenther F., Zimmermann S.,
RA   Heeg K., Mutters N.T., Nurjadi D.;
RT   "Molecular characterization of carbapenem-resistant Acinetobacter baumannii
RT   using whole-genome sequencing revealed missed transmission events, Germany,
RT   2012-2015.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN   [12] {ECO:0000313|EMBL:TPS01309.1, ECO:0000313|Proteomes:UP000318526, ECO:0000313|Proteomes:UP000320596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSN337038 {ECO:0000313|EMBL:TPS84755.1,
RC   ECO:0000313|Proteomes:UP000318526}, and MRSN7460
RC   {ECO:0000313|EMBL:TPS01309.1, ECO:0000313|Proteomes:UP000320596};
RA   Mcgann P., Snesrud E., Galac M.R.;
RT   "A Diverse Panel of Clinical Acinetobacter baumannii for Research Use.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00015829}.
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:0000256|HAMAP-Rule:MF_00036,
CC         ECO:0000256|SAAS:SAAS01125460};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00036};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00832879}.
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:0000256|HAMAP-Rule:MF_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00575517}.
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DR   EMBL; CP021782; ASF76661.1; -; Genomic_DNA.
DR   EMBL; CP026125; AUT36896.1; -; Genomic_DNA.
DR   EMBL; MDWM01000084; ODP71357.1; -; Genomic_DNA.
DR   EMBL; LYKI01000067; OIG67468.1; -; Genomic_DNA.
DR   EMBL; LYKQ01000058; OIH04575.1; -; Genomic_DNA.
DR   EMBL; NGCH01000812; OTL19830.1; -; Genomic_DNA.
DR   EMBL; NGEL01000030; OTM92370.1; -; Genomic_DNA.
DR   EMBL; QKWF01000059; PZM17994.1; -; Genomic_DNA.
DR   EMBL; SNVS01000059; TEX20686.1; -; Genomic_DNA.
DR   EMBL; SNVP01000101; TEX31091.1; -; Genomic_DNA.
DR   EMBL; VAFZ01000064; TLT61917.1; -; Genomic_DNA.
DR   EMBL; VHEA01000038; TPS01309.1; -; Genomic_DNA.
DR   EMBL; VHEY01000037; TPS84755.1; -; Genomic_DNA.
DR   RefSeq; WP_000199457.1; NZ_WBJK01000032.1.
DR   STRING; 470.IX87_04765; -.
DR   EnsemblBacteria; AKQ27505; AKQ27505; ACX60_12345.
DR   EnsemblBacteria; AMN00940; AMN00940; AZE33_07035.
DR   EnsemblBacteria; OBE58331; OBE58331; A7934_11960.
DR   EnsemblBacteria; ODP71357; ODP71357; BGC29_16755.
DR   KEGG; abaa:IX88_07955; -.
DR   KEGG; abw:BL01_15570; -.
DR   PATRIC; fig|470.1288.peg.2973; -.
DR   eggNOG; ENOG4105CIM; Bacteria.
DR   eggNOG; COG0013; LUCA.
DR   KO; K01872; -.
DR   OrthoDB; 91428at2; -.
DR   Proteomes; UP000094982; Unassembled WGS sequence.
DR   Proteomes; UP000179791; Unassembled WGS sequence.
DR   Proteomes; UP000179937; Unassembled WGS sequence.
DR   Proteomes; UP000194699; Unassembled WGS sequence.
DR   Proteomes; UP000194957; Unassembled WGS sequence.
DR   Proteomes; UP000197701; Chromosome.
DR   Proteomes; UP000236385; Chromosome.
DR   Proteomes; UP000248662; Unassembled WGS sequence.
DR   Proteomes; UP000297480; Unassembled WGS sequence.
DR   Proteomes; UP000297782; Unassembled WGS sequence.
DR   Proteomes; UP000309525; Unassembled WGS sequence.
DR   Proteomes; UP000318526; Unassembled WGS sequence.
DR   Proteomes; UP000320596; Unassembled WGS sequence.
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   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_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   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:SAAS00249969};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250154}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00299154};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00249928,
KW   ECO:0000313|EMBL:PZM17994.1};
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:SAAS00250206};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250204};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250135};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250194};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00423813}.
FT   DOMAIN          1..713
FT                   /note="AA_TRNA_LIGASE_II_ALA"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
FT   COILED          344..364
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          366..386
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          736..763
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   METAL           562
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   METAL           566
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   METAL           670
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT   METAL           674
FT                   /note="Zinc"
FT                   /evidence="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
//