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Database: UniProt
Entry: A0A1B2M2C1_9GAMM
LinkDB: A0A1B2M2C1_9GAMM
Original site: A0A1B2M2C1_9GAMM 
ID   A0A1B2M2C1_9GAMM        Unreviewed;       431 AA.
AC   A0A1B2M2C1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Histidine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00127};
DE            EC=6.1.1.21 {ECO:0000256|HAMAP-Rule:MF_00127};
DE   AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00127};
DE            Short=HisRS {ECO:0000256|HAMAP-Rule:MF_00127};
GN   Name=hisS {ECO:0000256|HAMAP-Rule:MF_00127};
GN   ORFNames=BFG52_13680 {ECO:0000313|EMBL:AOA59301.1};
OS   Acinetobacter larvae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1789224 {ECO:0000313|EMBL:AOA59301.1, ECO:0000313|Proteomes:UP000093391};
RN   [1] {ECO:0000313|EMBL:AOA59301.1, ECO:0000313|Proteomes:UP000093391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRTC-1 {ECO:0000313|EMBL:AOA59301.1,
RC   ECO:0000313|Proteomes:UP000093391};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC         histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC         Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001137, ECO:0000256|HAMAP-
CC         Rule:MF_00127};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_00127}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00127}.
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DR   EMBL; CP016895; AOA59301.1; -; Genomic_DNA.
DR   RefSeq; WP_067557387.1; NZ_CP016895.1.
DR   AlphaFoldDB; A0A1B2M2C1; -.
DR   STRING; 1789224.BFG52_13680; -.
DR   KEGG; ala:BFG52_13680; -.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000093391; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   HAMAP; MF_00127; His_tRNA_synth; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR015807; His-tRNA-ligase.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/HisZ.
DR   NCBIfam; TIGR00442; hisS; 1.
DR   PANTHER; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00127};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00127};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00127};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00127}; Reference proteome {ECO:0000313|Proteomes:UP000093391}.
FT   DOMAIN          21..320
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   431 AA;  48363 MW;  579FAF2CFFFF7695 CRC64;
     MSSIVAIKGF NDILPSQTPA WRRLEQQLAS LMDAYGYQQI RLPMVEHTHL FKRSIGDATD
     IVEKEMYTFL DKGNPPESLT LRPEGTAGCV RAMLEHNLLR GATPRVWYNG PMFRYEKPQK
     GRYRQFHQFG VETFGVATPD MDAELILLTA RLWKRLGISD KVQLELNSLG ESDERAAYRD
     ALVNFLSAHK ADLDEDSQRR LGTNPLRILD SKDANTQKIL EHAPKLHDFL QQESLQHFAQ
     LQQYLQAAGI DFVINQKLVR GLDYYNKTVF EWTTTHLGSQ GTVCAGGRYD GLVGQLKGKA
     EQSVPAVGFA MGIERLLLLL EQVAQDEVQR DCEVFLLADV AYQMQALVLA ENIRDQLEQA
     GSSIRLKVGS AGSMKSQMKK ADQSGAIYAL ILGEREWDAQ QLTVKTLANA DQSTVAIAEI
     STFLQQQLSS R
//
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