ID   SYH2_BACC1              Reviewed;         423 AA.
AC   P62370;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Histidine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00127};
DE            EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE   AltName: Full=Histidyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00127};
DE            Short=HisRS 2 {ECO:0000255|HAMAP-Rule:MF_00127};
GN   Name=hisS2 {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=BCE_4486;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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:0000255|HAMAP-Rule:MF_00127};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR   EMBL; AE017194; AAS43387.1; -; Genomic_DNA.
DR   RefSeq; WP_000027087.1; NC_003909.8.
DR   AlphaFoldDB; P62370; -.
DR   SMR; P62370; -.
DR   EnsemblBacteria; AAS43387; AAS43387; BCE_4486.
DR   GeneID; 59155028; -.
DR   GeneID; 64199746; -.
DR   KEGG; bca:BCE_4486; -.
DR   HOGENOM; CLU_025113_1_1_9; -.
DR   OMA; CDFDFIG; -.
DR   Proteomes; UP000002527; 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   CDD; cd00859; HisRS_anticodon; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 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   InterPro; IPR033656; HisRS_anticodon.
DR   PANTHER; PTHR43707; PTHR43707; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00442; hisS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..423
FT                   /note="Histidine--tRNA ligase 2"
FT                   /id="PRO_0000136096"
SQ   SEQUENCE   423 AA;  47777 MW;  A020C1D39ACF557E CRC64;
     MSIQIPRGTQ DILPGTVELW QYIEGQAREI CRRYNYKEIR TPIFEHTELF LRGVGDTTDI
     VQKEMYSFQD RGERSLTLRP EGTAPVVRSY VENKMFGDAT QPTKLYYIGQ MFRYERPQAG
     RYRQFVQFGI EAIGSNDPAI DAEVIALAVE FYRGMGLKNI KVVLNSLGDA ASRQAHRDAL
     IAHFEPRIGE FCSDCQSRLE KNPLRILDCK KDRNHELMGT APSITEYLNE DSAVYYEKVQ
     ELLTMMDVPF EKDPNLVRGL DYYQHTVFEI MSEAEGFGAI TTLSGGGRYN GLVQEIGGPE
     MPGIGFAMSI ERLIMALKAE NIELPIEHSI DCYVVALGEK AKDHAAKVAF DLRKAGLSVE
     KDYLDRKMKA QFKSADRLKA KFVAVLGEDE LDKGIINLKD MATGEQEEVA LDVFASYVAE
     KLI