ID A0A059ZTE3_ACIBA Unreviewed; 878 AA. AC A0A059ZTE3; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 11-NOV-2015, entry version 15. 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 ECO:0000313|EMBL:CRL93865.1}; GN ORFNames=ABCIP7010_1144 {ECO:0000313|EMBL:CRL93865.1}, ABR2090_2420 GN {ECO:0000313|EMBL:CRX65336.1}, ACX60_12345 GN {ECO:0000313|EMBL:AKQ27505.1}, AKG97_17310 GN {ECO:0000313|EMBL:KOP84734.1}, LH92_05680 GN {ECO:0000313|EMBL:KGF59377.1}, RQ37_17560 GN {ECO:0000313|EMBL:KJE57186.1}, RQ42_17590 GN {ECO:0000313|EMBL:KJE57151.1}, RQ49_13880 GN {ECO:0000313|EMBL:KJF11490.1}, RQ64_14245 GN {ECO:0000313|EMBL:KJF09521.1}, RQ82_10760 GN {ECO:0000313|EMBL:KJG74254.1}, RQ85_07295 GN {ECO:0000313|EMBL:KHX50032.1}, RQ98_13555 GN {ECO:0000313|EMBL:KJE69651.1}, RR20_14500 GN {ECO:0000313|EMBL:KJE65061.1}, RR27_13600 GN {ECO:0000313|EMBL:KJE70549.1}, RW49_09885 GN {ECO:0000313|EMBL:KHT87263.1}, RW53_10290 GN {ECO:0000313|EMBL:KHT72979.1}, RW56_13355 GN {ECO:0000313|EMBL:KHV19248.1}, RW57_13055 GN {ECO:0000313|EMBL:KHV24895.1}, RW58_10455 GN {ECO:0000313|EMBL:KHV34627.1}, RW59_15070 GN {ECO:0000313|EMBL:KHV12554.1}, RW60_15450 GN {ECO:0000313|EMBL:KHV29702.1}, TE32_12855 GN {ECO:0000313|EMBL:AKJ46435.1}, UN98_00130 GN {ECO:0000313|EMBL:KKZ42688.1}; OS Acinetobacter baumannii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=470 {ECO:0000313|EMBL:KHX50032.1}; RN [1] {ECO:0000313|EMBL:KGF59377.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MAR002 {ECO:0000313|EMBL:KGF59377.1}; RA Alvarez-Fraga L., Rumbo-Feal S., Merino M., Bou G., Poza M.; RT "Complete genome of a biofilm superproducing strain of Acinetobacter RT baumannii."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. 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|EMBL:KKZ42688.1, ECO:0000313|Proteomes:UP000033888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LUH_7841 {ECO:0000313|EMBL:KKZ42688.1, RC ECO:0000313|Proteomes:UP000033888}; RA Sahl J., Zarrilli R.; RT "Genomic epidemiology of Acinetobacter baumannii strains assigned to RT the ST25 clonal lineage; the evolution of a globally relevant clone."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:CRL93865.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP70.10 {ECO:0000313|EMBL:CRL93865.1}, and R2090 RC {ECO:0000313|EMBL:CRX65336.1}; RA Wibberg Daniel; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:AKQ27505.1, ECO:0000313|Proteomes:UP000036024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17978-mff {ECO:0000313|EMBL:AKQ27505.1, RC 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 [6] {ECO:0000313|EMBL:KHX50032.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10441_14 {ECO:0000313|EMBL:KOP84734.1}, ABUH304350 RC {ECO:0000313|EMBL:KHV12554.1}, ABUH304352 RC {ECO:0000313|EMBL:KHV24895.1}, ABUH404571 RC {ECO:0000313|EMBL:KHV34627.1}, ABUH42783 RC {ECO:0000313|EMBL:KHT87263.1}, ABUH463346 RC {ECO:0000313|EMBL:KHV19248.1}, ABUH4837 {ECO:0000313|EMBL:KHT72979.1}, RC ABUH524354 {ECO:0000313|EMBL:KHV29702.1}, UH175_674 RC {ECO:0000313|EMBL:KJE70549.1}, UH225_433 RC {ECO:0000313|EMBL:KJG74254.1}, UH326_445 RC {ECO:0000313|EMBL:KHX50032.1}, UH381_484 RC {ECO:0000313|EMBL:KJE69651.1}, UH475_361 RC {ECO:0000313|EMBL:KJF09521.1}, UH514_289 RC {ECO:0000313|EMBL:KJF11490.1}, UH592_583 RC {ECO:0000313|EMBL:KJE65061.1}, UH66_253 {ECO:0000313|EMBL:KJE57186.1}, RC and UH66_271 {ECO:0000313|EMBL:KJE57151.1}; RA Tran T., Druce J.; RT "MeaNS - Measles Nucleotide Surveillance Program."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|Proteomes:UP000033888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LUH_7841 {ECO:0000313|Proteomes:UP000033888}; RG RefSeq; RL Submitted (SEP-2015) to UniProtKB. 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 (By similarity). {ECO:0000256|SAAS:SAAS00202356}. 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, ECO:0000256|SAAS:SAAS00202362}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00036, ECO:0000256|SAAS:SAAS00202362}; 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 --------------------------------------------------------------------------- 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; CP010779; AKJ46435.1; -; Genomic_DNA. DR EMBL; CP012004; AKQ27505.1; -; Genomic_DNA. DR EMBL; LN865143; CRL93865.1; -; Genomic_DNA. DR EMBL; LN868200; CRX65336.1; -; Genomic_DNA. DR EMBL; JRHB01000001; KGF59377.1; -; Genomic_DNA. DR EMBL; JWRT03000087; KHT72979.1; -; Genomic_DNA. DR EMBL; JWRU03000006; KHT87263.1; -; Genomic_DNA. DR EMBL; JWSF03000041; KHV12554.1; -; Genomic_DNA. DR EMBL; JWSE03000300; KHV19248.1; -; Genomic_DNA. DR EMBL; JWSH03000049; KHV24895.1; -; Genomic_DNA. DR EMBL; JWSI03000161; KHV29702.1; -; Genomic_DNA. DR EMBL; JWSJ03000099; KHV34627.1; -; Genomic_DNA. DR EMBL; JWUX03000030; KHX50032.1; -; Genomic_DNA. DR EMBL; JZIX02000037; KJE57151.1; -; Genomic_DNA. DR EMBL; JZIZ02000042; KJE57186.1; -; Genomic_DNA. DR EMBL; JZIY02000043; KJE65061.1; -; Genomic_DNA. DR EMBL; JZJA02000031; KJE69651.1; -; Genomic_DNA. DR EMBL; JZJB02000041; KJE70549.1; -; Genomic_DNA. DR EMBL; JZJF02000040; KJF09521.1; -; Genomic_DNA. DR EMBL; JZJG02000036; KJF11490.1; -; Genomic_DNA. DR EMBL; JWVA03000023; KJG74254.1; -; Genomic_DNA. DR EMBL; JZBX01000001; KKZ42688.1; -; Genomic_DNA. DR EMBL; LGYW01000079; KOP84734.1; -; Genomic_DNA. DR RefSeq; WP_000199457.1; NZ_LCTE01000045.1. DR STRING; 575584.HMPREF0010_03139; -. DR EnsemblBacteria; AIA53181; AIA53181; BL01_15570. DR EnsemblBacteria; AIL75110; AIL75110; IX88_07955. DR EnsemblBacteria; KFB62834; KFB62834; GQ86_11415. DR EnsemblBacteria; KGF59377; KGF59377; LH92_05680. DR EnsemblBacteria; KHX50032; KHX50032; RQ85_07295. DR KEGG; abaa:IX88_07955; -. DR KEGG; abw:BL01_15570; -. DR eggNOG; ENOG4105CIM; Bacteria. DR eggNOG; COG0013; LUCA. DR KO; K01872; -. DR Proteomes; UP000033888; Unassembled WGS sequence. DR Proteomes; UP000035522; Chromosome. DR Proteomes; UP000036024; 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:SAAS00015678}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015856}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033888, KW ECO:0000313|Proteomes:UP000035522}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00299154}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015738}; 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:SAAS00015761}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015671}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015783}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015697}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00015895}. 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 //