ID A0A059ZTE3_ACIBA Unreviewed; 878 AA. AC A0A059ZTE3; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 13-FEB-2019, entry version 49. 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_1 {ECO:0000313|EMBL:SSQ35668.1}; GN Synonyms=alaS {ECO:0000256|HAMAP-Rule:MF_00036, GN ECO:0000313|EMBL:ASF76661.1}, alaS_3 {ECO:0000313|EMBL:SSU38360.1}; GN ORFNames=A7M79_15050 {ECO:0000313|EMBL:OIH04575.1}, A7M90_08745 GN {ECO:0000313|EMBL:OIG67468.1}, AB719_03830 GN {ECO:0000313|EMBL:RDJ61772.1}, 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}, CEJ63_18835 GN {ECO:0000313|EMBL:PAM66189.1}, CYQ93_21680 GN {ECO:0000313|EMBL:RIL13137.1}, D3X67_02220 GN {ECO:0000313|EMBL:RJN72249.1}, DOL94_06455 GN {ECO:0000313|EMBL:PZM17994.1}, SAMEA104305229_03711 GN {ECO:0000313|EMBL:SSQ35668.1}, SAMEA104305292_02110 GN {ECO:0000313|EMBL:SSS44900.1}, SAMEA104305325_02884 GN {ECO:0000313|EMBL:SST96056.1}, SAMEA104305337_09813 GN {ECO:0000313|EMBL:SSU38360.1}; 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:RDJ61772.1, ECO:0000313|Proteomes:UP000254935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KMDRAB19 {ECO:0000313|EMBL:RDJ61772.1, RC ECO:0000313|Proteomes:UP000254935}; RA Feng Y., Chiu C.-H.; RT "Genome analysis of of clinical invasive Acinetobacter baumannii RT isolates in Taiwan."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {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 [3] {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 RT of Acinetobacter baumannii."; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. RN [4] {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 [5] {ECO:0000313|EMBL:PAM66189.1, ECO:0000313|Proteomes:UP000216072} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB75 {ECO:0000313|EMBL:PAM66189.1, RC ECO:0000313|Proteomes:UP000216072}; RA Chen Q.; RT "Carbapenem-resistant Acinetobacter baumannii strains."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. RN [6] {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 RT belonging to global clone 1 (GC1)."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:AUT36896.1, ECO:0000313|Proteomes:UP000236385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT36896.1, RC ECO:0000313|Proteomes:UP000236385}; 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 [8] {ECO:0000313|EMBL:AUT36896.1, ECO:0000313|Proteomes:UP000236385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT36896.1, RC ECO:0000313|Proteomes:UP000236385}; 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:RIL13137.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=APC25 {ECO:0000313|EMBL:RIL13137.1}; RA Freitas D.Y., Araujo S., Folador A.R.C., Ramos R.T.J., Azevedo J.S.N., RA Tacao M., Silva A., Henriques I., Barauna R.A.; RT "Extended spectrum beta-lactamase-producing Gram-negative bacteria RT recovered from an Amazonian mesotrophic lake."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [10] {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 RT in an hospital from French Polynesia."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|Proteomes:UP000262639, ECO:0000313|Proteomes:UP000263147, ECO:0000313|Proteomes:UP000263963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4300STDY7045733 {ECO:0000313|EMBL:SSQ35668.1, RC ECO:0000313|Proteomes:UP000263963}, 4300STDY7045797 RC {ECO:0000313|EMBL:SSS44900.1, ECO:0000313|Proteomes:UP000262639}, RC 4300STDY7045830 {ECO:0000313|EMBL:SST96056.1, RC ECO:0000313|Proteomes:UP000264417}, and 4300STDY7045842 RC {ECO:0000313|EMBL:SSU38360.1, ECO:0000313|Proteomes:UP000263147}; RG Pathogen Informatics; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:RJN72249.1, ECO:0000313|Proteomes:UP000265486} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC47 {ECO:0000313|EMBL:RJN72249.1, RC ECO:0000313|Proteomes:UP000265486}; RA Cerezales M., Xanthopoulou K., Ertel J., Bustamante Z., Seifert H., RA Gallego L., Higgins P.G.; RT "Acinetobacter baumannii analysis by core genome MLST in two hospitals RT in Bolivia: endemicity of international clone 7 isolates."; RL Submitted (SEP-2018) 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:SAAS00015829}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L- CC alanyl-tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, CC Rhea:RHEA-COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, CC ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00036, ECO:0000256|SAAS:SAAS01125460}; 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:SAAS00832879}. 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:SAAS00575517}. 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; 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; NKKG01000086; PAM66189.1; -; Genomic_DNA. DR EMBL; QKWF01000059; PZM17994.1; -; Genomic_DNA. DR EMBL; LFHE01000033; RDJ61772.1; -; Genomic_DNA. DR EMBL; PYSX01000042; RIL13137.1; -; Genomic_DNA. DR EMBL; QXPA01000005; RJN72249.1; -; Genomic_DNA. DR EMBL; UFJW01000100; SSQ35668.1; -; Genomic_DNA. DR EMBL; UFLY01000010; SSS44900.1; -; Genomic_DNA. DR EMBL; UFNA01000142; SST96056.1; -; Genomic_DNA. DR EMBL; UFNQ01000059; SSU38360.1; -; Genomic_DNA. DR RefSeq; WP_000199457.1; NZ_ULHD01000017.1. 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 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; UP000216072; Unassembled WGS sequence. DR Proteomes; UP000236385; Chromosome. DR Proteomes; UP000248662; Unassembled WGS sequence. DR Proteomes; UP000254935; Unassembled WGS sequence. DR Proteomes; UP000262639; Unassembled WGS sequence. DR Proteomes; UP000263147; Unassembled WGS sequence. DR Proteomes; UP000263963; Unassembled WGS sequence. DR Proteomes; UP000264417; Unassembled WGS sequence. DR Proteomes; UP000265486; 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:SAAS00467511, ECO:0000313|EMBL:RDJ61772.1}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00467523}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000094982, KW ECO:0000313|Proteomes:UP000179791, ECO:0000313|Proteomes:UP000179937, KW ECO:0000313|Proteomes:UP000194699}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00467678}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00467503, ECO:0000313|EMBL:PZM17994.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015702}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00467669}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00467606}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00467527}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00467491}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00015895}. FT DOMAIN 1 713 AA_TRNA_LIGASE_II_ALA. FT {ECO:0000259|PROSITE:PS50860}. FT COILED 344 364 {ECO:0000256|SAM:Coils}. FT COILED 366 386 {ECO:0000256|SAM:Coils}. 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 //