ID A0A059ZTE3_ACIBA Unreviewed; 878 AA. AC A0A059ZTE3; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 27-MAY-2015, entry version 10. 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=BL01_15570 {ECO:0000313|EMBL:AIA53181.1}, 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}, 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}, SF14_16890 GN {ECO:0000313|EMBL:KJC88127.1}, SG88_14990 GN {ECO:0000313|EMBL:KJC73038.1}, SG89_17820 GN {ECO:0000313|EMBL:KJC97589.1}, SG90_14800 GN {ECO:0000313|EMBL:KJD10253.1}, SG91_17790 GN {ECO:0000313|EMBL:KJC66248.1}, SG92_15905 GN {ECO:0000313|EMBL:KJD03680.1}, SG93_16010 GN {ECO:0000313|EMBL:KJC77816.1}, SG94_16180 GN {ECO:0000313|EMBL:KJD07771.1}, SG95_17030 GN {ECO:0000313|EMBL:KJC84273.1}, SG96_14110 GN {ECO:0000313|EMBL:KJC97146.1}, SG97_15805 GN {ECO:0000313|EMBL:KJC91421.1}, SG98_16445 GN {ECO:0000313|EMBL:KJC79922.1}, SG99_16475 GN {ECO:0000313|EMBL:KJC68487.1}; 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, ECO:0000313|Proteomes:UP000027328}; 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:KHX50032.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UH175_674 {ECO:0000313|EMBL:KJE70549.1}, 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 Adams M., Brinkac L., Sanka R., Wright M., Sutton G., Bonomo R., RA Jacobs M.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KJC66248.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORAB01 {ECO:0000313|EMBL:KJD10253.1}, ORAB02 RC {ECO:0000313|EMBL:KJD03680.1}, ORAB03 {ECO:0000313|EMBL:KJD07771.1}, RC ORAB08 {ECO:0000313|EMBL:KJC88127.1}, ORAB09 RC {ECO:0000313|EMBL:KJC84273.1}, ORAB10 {ECO:0000313|EMBL:KJC97146.1}, RC ORAB13 {ECO:0000313|EMBL:KJC77816.1}, ORAB14 RC {ECO:0000313|EMBL:KJC79922.1}, ORAB15 {ECO:0000313|EMBL:KJC68487.1}, RC ORAB16 {ECO:0000313|EMBL:KJC97589.1}, ORAB17 RC {ECO:0000313|EMBL:KJC73038.1}, ORAB18 {ECO:0000313|EMBL:KJC66248.1}, RC and ORAB19 {ECO:0000313|EMBL:KJC91421.1}; RA Adams M., Brinkac L., Sanka R., Wright M., Sutton G., Bonomo R., RA Buser G., Beldavs Z., Pfeiffer C., Cassidy M., Cunningham M., RA Tierheimer J., Rudin S.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:AIA53181.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AC29 {ECO:0000313|EMBL:AIA53181.1}; RA Lean S.S., Suhaili Z., Yeo C.C., Thong K.-L.; RT "Comparative genomics of polymyxin-resistant and susceptible RT Acinetobacter baumannii isolated from the same patient."; RL Submitted (APR-2015) 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 (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; CP007535; AIA53181.1; -; Genomic_DNA. DR EMBL; JRHB01000001; KGF59377.1; -; Genomic_DNA. DR EMBL; JWUX02000138; KHX50032.1; -; Genomic_DNA. DR EMBL; JZCE01000044; KJC66248.1; -; Genomic_DNA. DR EMBL; JZCH01000045; KJC68487.1; -; Genomic_DNA. DR EMBL; JZCF01000030; KJC73038.1; -; Genomic_DNA. DR EMBL; JZCJ01000039; KJC77816.1; -; Genomic_DNA. DR EMBL; JZCI01000034; KJC79922.1; -; Genomic_DNA. DR EMBL; JZCL01000037; KJC84273.1; -; Genomic_DNA. DR EMBL; JZCM01000037; KJC88127.1; -; Genomic_DNA. DR EMBL; JZCD01000038; KJC91421.1; -; Genomic_DNA. DR EMBL; JZCK01000033; KJC97146.1; -; Genomic_DNA. DR EMBL; JZCG01000046; KJC97589.1; -; Genomic_DNA. DR EMBL; JZCO01000036; KJD03680.1; -; Genomic_DNA. DR EMBL; JZCN01000034; KJD07771.1; -; Genomic_DNA. DR EMBL; JZCP01000031; KJD10253.1; -; Genomic_DNA. DR EMBL; JZIX01000037; KJE57151.1; -; Genomic_DNA. DR EMBL; JZIZ01000042; KJE57186.1; -; Genomic_DNA. DR EMBL; JZIY01000043; KJE65061.1; -; Genomic_DNA. DR EMBL; JZJA01000031; KJE69651.1; -; Genomic_DNA. DR EMBL; JZJB01000041; KJE70549.1; -; Genomic_DNA. DR EMBL; JZJF01000038; KJF09521.1; -; Genomic_DNA. DR EMBL; JZJG01000044; KJF11490.1; -; Genomic_DNA. DR RefSeq; WP_000199457.1; NZ_KN708516.1. DR ProteinModelPortal; A0A059ZTE3; -. 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; KHT72979; KHT72979; RW53_10290. DR EnsemblBacteria; KHT87263; KHT87263; RW49_09885. DR EnsemblBacteria; KHV12554; KHV12554; RW59_15070. DR EnsemblBacteria; KHV19248; KHV19248; RW56_13355. DR EnsemblBacteria; KHV21643; KHV21643; RW63_13075. DR EnsemblBacteria; KHV24895; KHV24895; RW57_13055. DR EnsemblBacteria; KHV29702; KHV29702; RW60_15450. DR EnsemblBacteria; KHV34627; KHV34627; RW58_10455. DR EnsemblBacteria; KHV36417; KHV36417; RW62_16080. DR Proteomes; UP000027328; 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}; KW Complete proteome {ECO:0000313|Proteomes:UP000027328}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015877}; 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 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 //