ID   A0A059ZTE3_ACIBA        Unreviewed;       878 AA.
AC   A0A059ZTE3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   01-APR-2015, entry version 8.
DE   SubName: Full=Alanyl-tRNA synthetase {ECO:0000313|EMBL:KHV21643.1};
GN   Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036};
GN   ORFNames=LH92_05680 {ECO:0000313|EMBL:KGF59377.1}, RQ85_07295
GN   {ECO:0000313|EMBL:KHX50032.1}, RW49_09885
GN   {ECO:0000313|EMBL:KHT87263.1}, 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}, RW62_16080
GN   {ECO:0000313|EMBL:KHV36417.1}, RW63_13075
GN   {ECO:0000313|EMBL:KHV21643.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:KHV21643.1};
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:KHV21643.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ABUH16665 {ECO:0000313|EMBL:KHV36417.1}, ABUH222351
RC   {ECO:0000313|EMBL:KHV21643.1}, 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}, ABUH524354
RC   {ECO:0000313|EMBL:KHV29702.1}, and UH326_445
RC   {ECO:0000313|EMBL:KHX50032.1};
RA   Adams M., Brinkac L., Sanka R., Wright M., Sutton G., Bonomo R.,
RA   Jacobs M.;
RL   Submitted (DEC-2014) 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: 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:SAAS00166766};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00036, ECO:0000256|SAAS:SAAS00166766};
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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KHV21643.1}.
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DR   EMBL; JRHB01000001; KGF59377.1; -; Genomic_DNA.
DR   EMBL; JWRU01000039; KHT87263.1; -; Genomic_DNA.
DR   EMBL; JWSF01000043; KHV12554.1; -; Genomic_DNA.
DR   EMBL; JWSE01000040; KHV19248.1; -; Genomic_DNA.
DR   EMBL; JWSG01000034; KHV21643.1; -; Genomic_DNA.
DR   EMBL; JWSH01000033; KHV24895.1; -; Genomic_DNA.
DR   EMBL; JWSI01000041; KHV29702.1; -; Genomic_DNA.
DR   EMBL; JWSJ01000029; KHV34627.1; -; Genomic_DNA.
DR   EMBL; JWSK01000062; KHV36417.1; -; Genomic_DNA.
DR   EMBL; JWUX01000139; KHX50032.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0A059ZTE3; -.
DR   EnsemblBacteria; AIA53181; AIA53181; BL01_15570.
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   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
//