ID   SYP_THEP1               Reviewed;         577 AA.
AC   A5IJQ9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=Tpet_0408;
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000702; ABQ46432.1; -; Genomic_DNA.
DR   RefSeq; WP_011943057.1; NC_009486.1.
DR   AlphaFoldDB; A5IJQ9; -.
DR   SMR; A5IJQ9; -.
DR   STRING; 390874.Tpet_0408; -.
DR   EnsemblBacteria; ABQ46432; ABQ46432; Tpet_0408.
DR   KEGG; tpt:Tpet_0408; -.
DR   eggNOG; COG0442; Bacteria.
DR   HOGENOM; CLU_016739_0_0_0; -.
DR   OMA; NCDYAAN; -.
DR   Proteomes; UP000006558; Chromosome.
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; cd00861; ProRS_anticodon_short; 1.
DR   CDD; cd00779; ProRS_core_prok; 1.
DR   Gene3D; 3.30.930.10; -; 2.
DR   Gene3D; 3.40.50.800; -; 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   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF04073; tRNA_edit; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   SUPFAM; SSF55826; SSF55826; 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..577
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_1000069171"
SQ   SEQUENCE   577 AA;  66003 MW;  8E5FAA27B708EB08 CRC64;
     MRMKDLYAPT LKETPSDVET VSHEYLLRGG FIRKVAAGIY TYLPLGRRVL LKIENIVREE
     MNRIGAQEIL MPILQPAELW KQSGRWDDYG PEMMKLKDRH ERDFTLGPTH EEIVTDLVKN
     ELRSYKQLPL TLYQIANKYR DEIRPRFGLL RAREFIMKDA YSFHASWESL DETYEEFKKA
     YSRIMERLGV RYMIIEAETG AIGGNASHEF VVPAKIGETN VLFCEKCGYQ ASDEKAEYRG
     EYTQEQEKEK TLEKVPTPGV KTIEEVSKFL GVSPSKIVKS LLYKGREGYV MVLIRGDLEL
     NEAKLKAHLK DQSLRMATPE EILKDFGVPV GFIGPIGVDV KKVADHSVRG LKNFVVGGME
     EDTHYVNANH PRDFKVDEWY DLRTMVEGDP CPVCGEPLKA TKGIELGHIF KLGTKYSEAM
     KAYFMDENGE MKPFIMGCYG WGVSRTMAAV VEHFHDENGM IWPLSIAPYT VVVDILNMND
     AEQKQVGEKI YQVLSEKGEE VVLDDREVSP GFKFKDADLI GFPIRINVGR SLKEGVVELK
     KRYSKELVKV NIKNGFGTLL ETLEKMKREY DPKEAAR