ID SYP_CAMJR Reviewed; 569 AA.
AC Q5HVM3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01569};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01569};
DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01569};
GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01569}; OrderedLocusNames=CJE0647;
OS Campylobacter jejuni (strain RM1221).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM1221;
RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA Nelson K.E.;
RT "Major structural differences and novel potential virulence mechanisms from
RT the genomes of multiple Campylobacter species.";
RL PLoS Biol. 3:72-85(2005).
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). As ProRS can
CC inadvertently accommodate and process non-cognate amino acids such as
CC alanine and cysteine, to avoid such errors it has two additional
CC distinct editing activities against alanine. One activity is designated
CC as 'pretransfer' editing and involves the tRNA(Pro)-independent
CC hydrolysis of activated Ala-AMP. The other activity is designated
CC 'posttransfer' editing and involves deacylation of mischarged Ala-
CC tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
CC {ECO:0000255|HAMAP-Rule:MF_01569}.
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_01569};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01569}.
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC editing domain and the C-terminal anticodon-binding domain.
CC {ECO:0000255|HAMAP-Rule:MF_01569}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}.
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DR EMBL; CP000025; AAW35840.1; -; Genomic_DNA.
DR RefSeq; WP_011049735.1; NC_003912.7.
DR AlphaFoldDB; Q5HVM3; -.
DR SMR; Q5HVM3; -.
DR KEGG; cjr:CJE0647; -.
DR HOGENOM; CLU_016739_0_0_7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
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; cd04334; ProRS-INS; 1.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_01569; Pro_tRNA_synth_type1; 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; IPR023717; Pro-tRNA-Synthase_IIa_type1.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR033730; ProRS_core_prok.
DR InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR NCBIfam; TIGR00409; proS_fam_II; 1.
DR PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42753:SF2; PROLINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF04073; tRNA_edit; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55826; YbaK/ProRS associated domain; 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..569
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000248664"
SQ SEQUENCE 569 AA; 64524 MW; 9A186ED4850DEFA8 CRC64;
MMRFTKFYAP SLKEAPKDAS LPSHIFLTRA GFVEQIGSGL YNFLPLGKRV LDKIKNIVKE
EMDKAGAQEV NLSFITPASL WQESGRYNVF GKELLRFKDR KENEFVLGPT HEEAMLSLVK
NKITSYKQLP LHLYQIGLKF RDEARPRFGL LRCREFLMKD GYSFHANEED LGREFELMYK
TYSQILQRMG LDFRAVEADS GAIGGSGSKE FMVLAKNGED DILICENCDY AANVEAAKRA
KKTCQDERPE ANYASKFHTP NIKTIDSLAQ FFKINAFYTI KAVVKKAIYE NESKLVVFFI
RGSDDLQEVK AQNACSALEL VDASEEELEK AGLVAGFIGF VGLKDIDFYI DFELENEKQM
IMGANEKDYH LIGIDVVNLN KDRFKDLIEV KEGDCCVKCG AKLKQSKGIE VGHIFKLGQK
YSKAMNANFL DENGKSQPFY MGCYGIGVSR LLAVATEASH DEKGCIWNKT LAPFVLEIIV
SNLKDEKALE FANKLYEDLT NLGLEVLLDD RNERFGVKMN DFELMGFPYA LVVGKGLEKN
EIELIQREGL IKELIKTDEL MEILKKKVL
//
