ID   A0A438XAF7_HELPX        Unreviewed;       442 AA.
AC   A0A438XAF7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   07-APR-2021, entry version 7.
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=EC546_07870 {ECO:0000313|EMBL:RVZ33320.1};
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210 {ECO:0000313|EMBL:RVZ33320.1, ECO:0000313|Proteomes:UP000288780};
RN   [1] {ECO:0000313|EMBL:RVZ33320.1, ECO:0000313|Proteomes:UP000288780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZH96 {ECO:0000313|EMBL:RVZ33320.1,
RC   ECO:0000313|Proteomes:UP000288780};
RA   Wagner K.;
RT   "Genetic determinants and prediction of antibiotic resistance phenotypes in
RT   Helicobacter pylori.";
RL   Submitted (OCT-2018) 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|HAMAP-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RVZ33320.1}.
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DR   EMBL; RJHJ01000027; RVZ33320.1; -; Genomic_DNA.
DR   Proteomes; UP000288780; Unassembled WGS sequence.
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; 3.40.50.800; -; 1.
DR   HAMAP; MF_00127; His_tRNA_synth; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
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   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   TIGRFAMs; TIGR00442; hisS; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00127}; Coiled coil {ECO:0000256|SAM:Coils};
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   ECO:0000313|EMBL:RVZ33320.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00127};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00127}.
FT   DOMAIN          1..379
FT                   /note="AA_TRNA_LIGASE_II"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          237..257
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   442 AA;  50233 MW;  2EF0AAA5995FE227 CRC64;
     MITPKVLSGF KDRLPKDAIQ KAQLLSKVSV VFQSFGFVPI ETPHLEYAEV LLPDASSDIQ
     KEIYRFKDHG DRDVALRFDL TVPLARFVSL HHQTLGMPFK RYAIGNVFRG ERAQKGRYRE
     FTQCDFDFIG SESLVCDAEI VQVIIASLKA LDLEDFCISI NHRKILNGIC EYFGVSQVNE
     ALRIVDKLEK IGLNGVEEEL KKECDLDLNT IKELLEMVQI KQNDLSHAEF FEKIAYLKDY
     NENLKKGIQD LERLYQLLGD LQISQNLYKI DFSIARGLGY YTGIVYETTL NGMKSLGSVC
     SGGRYDHLTK NFSKENLQGV GASIGIDRLI VALSEMQLLD ERSTQAKVLI ACMHEEYFSY
     ANRLAESLRQ SGIFSEVYPE AQKIKKPFSY ANHRGHEFVA VIGEEEFKSE TLSLKNMHSG
     MQLNCLSFLK ALEIIGENDE DL
//