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}. 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; 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 //