SYP_BARHE
ID SYP_BARHE Reviewed; 441 AA.
AC Q6G3A4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01570};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01570};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01570};
DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01570};
GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01570}; OrderedLocusNames=BH08790;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-
CC step reaction: proline is first activated by ATP to form Pro-AMP and
CC then transferred to the acceptor end of tRNA(Pro). {ECO:0000255|HAMAP-
CC Rule:MF_01570}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC EC=6.1.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01570};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01570}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01570}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01570}.
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DR EMBL; BX897699; CAF27677.1; -; Genomic_DNA.
DR RefSeq; WP_011180772.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q6G3A4; -.
DR SMR; Q6G3A4; -.
DR STRING; 283166.BH08790; -.
DR PaxDb; Q6G3A4; -.
DR PRIDE; Q6G3A4; -.
DR EnsemblBacteria; CAF27677; CAF27677; BH08790.
DR GeneID; 64157119; -.
DR KEGG; bhe:BH08790; -.
DR eggNOG; COG0442; Bacteria.
DR OMA; NCDYAAN; -.
DR Proteomes; UP000000421; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_01570; Pro_tRNA_synth_type2; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
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; IPR002316; Pro-tRNA-ligase_IIa.
DR InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR InterPro; IPR023716; Prolyl-tRNA_ligase_IIa_type2.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR033730; ProRS_core_prok.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00409; proS_fam_II; 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..441
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000248889"
SQ SEQUENCE 441 AA; 50439 MW; 9D9ECFCFD9DF031A CRC64;
MRLSQYFLPL LKENPKEAEI ISHRLMLRAG MIRQQTSGIY SWLPLGKKVL DKICKIIREE
QERAGAIEIL MPTIQSADLW RESDRYDDYG LEMLRIKDRQ KRDLLYGPTN EEMVTDIFRS
YIRSYKDLPL NLYHIQWKFR DEIRPRFGVM RSREFLMKDA YSFDLDYEGS KISYNRMFVA
YLRTFSCLGL KAIPMRADTG PIGGKLSHEF IILAETGESA IFCDKHFLEL TVPDSSIDFS
DKAILANIVK QWTSFYAATE EMHDEEEWAK ISDNNRLSAR GIEVGHIFHF GTKYSAPMGA
KVMGQDGKEH LVSMGSYGIG PSRLVAAVIE ASHDENGIIW PKSIAPFDFG IINMKPDDEK
CTHACETLYK GLRYAGFDPL LDDRNERPGS KFATMDLIGL PTQIIVGPKS VAQNEVEIKD
RKTGIKKSLT VENVLNQFSV I