SYH_BARBK
ID SYH_BARBK Reviewed; 496 AA.
AC A1UTY3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127};
GN OrderedLocusNames=BARBAKC583_1178;
OS Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-2006) 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: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; CP000524; ABM45003.1; -; Genomic_DNA.
DR RefSeq; WP_005767850.1; NC_008783.1.
DR AlphaFoldDB; A1UTY3; -.
DR SMR; A1UTY3; -.
DR STRING; 360095.BARBAKC583_1178; -.
DR EnsemblBacteria; ABM45003; ABM45003; BARBAKC583_1178.
DR KEGG; bbk:BARBAKC583_1178; -.
DR PATRIC; fig|360095.6.peg.1140; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_3_2_5; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000000643; 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 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; Reference proteome.
FT CHAIN 1..496
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000016314"
SQ SEQUENCE 496 AA; 55551 MW; A2D187B4C75783FD CRC64;
MSKKEEKTKV RLPRGFVDRT SAQLHALETM IAQIHEVYES YGFEALETPI FEYTDVLGKF
LPDSDRPNAG VFSLQDEDEQ WMSLRYDLTA PLARYFAENF EILPKPYRSY RSGFVFRNEK
PGPGRFRQFM QLDADIVGSS TVAADAEICM MAADSLERLG IQRHDYVIRL SNRKILDGVL
ELIGLQGDEQ AEKRLTILRA IDKFDKFGME GVRLLLGKGR LDESGDFTKG AGLSQQESEP
ILSLISVGAE TAEATLDNLK NIVGHTIRGL EGIHELEEMQ TIFSKNGYQD RIKIDPSVVR
GLDYYTGPVF EAELLFDVLN EEGQKVVFGS VGGGGRYDGL VARFRDEAVP ATGFSVGVSR
LMAALHNLGK CPVKKTVGPV VVLMMDKDPE YVAYYQKMVM QLRHAGIRSE LYLGAAGIKA
QMKYADRRHA PCVVIQGASE RQEGKVQIKD LIEGARLSAE IKDNQTWRES RPAQIMVDEN
QLVQAVQEIL VAHQFL