ID SYP_ENTFA Reviewed; 572 AA.
AC Q831W7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 124.
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=EF_2379;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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; AE016830; AAO82100.1; -; Genomic_DNA.
DR RefSeq; NP_816030.1; NC_004668.1.
DR RefSeq; WP_002382780.1; NZ_KE136528.1.
DR PDB; 2J3L; X-ray; 2.30 A; A/B=1-572.
DR PDB; 2J3M; X-ray; 2.30 A; A/B=1-572.
DR PDBsum; 2J3L; -.
DR PDBsum; 2J3M; -.
DR AlphaFoldDB; Q831W7; -.
DR SMR; Q831W7; -.
DR DIP; DIP-29057N; -.
DR STRING; 226185.EF_2379; -.
DR EnsemblBacteria; AAO82100; AAO82100; EF_2379.
DR KEGG; efa:EF2379; -.
DR PATRIC; fig|226185.45.peg.1159; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_016739_0_0_9; -.
DR BRENDA; 6.1.1.15; 2095.
DR EvolutionaryTrace; Q831W7; -.
DR Proteomes; UP000001415; 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:0016740; F:transferase activity; IEA:UniProt.
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 Gene3D; 3.90.960.10; YbaK/aminoacyl-tRNA synthetase-associated 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..572
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000248688"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 44..62
FT /evidence="ECO:0007829|PDB:2J3L"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 153..166
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 167..187
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:2J3L"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 302..309
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 319..326
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2J3M"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:2J3M"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:2J3L"
FT TURN 348..352
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:2J3L"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 396..415
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 437..444
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 445..456
FT /evidence="ECO:0007829|PDB:2J3L"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 472..478
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 483..498
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 512..522
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 532..536
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 538..543
FT /evidence="ECO:0007829|PDB:2J3L"
FT TURN 544..546
FT /evidence="ECO:0007829|PDB:2J3L"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:2J3L"
FT HELIX 554..564
FT /evidence="ECO:0007829|PDB:2J3L"
SQ SEQUENCE 572 AA; 64267 MW; D2267BE6E4A85998 CRC64;
MKQSKMLIPT LREVPNDAEV LSHQILLRAG YIRQVAAGIY SYLPLANRVL EKLKTIMREE
FEKIDAVEML MPALLPAELW KESGRYETYG PNLYRLKDRN DRDYILGPTH EETFTELIRD
EINSYKRLPL NLYQIQTKYR DEKRSRSGLL RGREFIMKDG YSFHADEASL DQSYRDYEKA
YSRIFERCGL EFRAIIGDGG AMGGKDSKEF MAISEIGEDT ICYSTESDYA ANLEMATSLY
TPKKSHETQL DLEKIATPEV GTIAEVANFF EVEPQRIIKS VLFIADEEPV MVLVRGDHDV
NDVKLKNFLG ADFLDEATEE DARRVLGAGF GSIGPVNVSE DVKIYADLAV QDLANAIVGA
NEDGYHLTNV NPDRDFQPIS YEDLRFVQEG DPSPDGNGVL AFTKGIEIGH IFKLGTRYSD
AMGATVLDEN GREKSVIMGC YGIGVSRLLS AIVEQNADER GINWPTGIAP FDLHVVQMNV
KDEYQTKLSQ EVEAMMTEAG YEVLVDDRNE RAGVKFADAD LIGCPIRITV GKKAVDGVVE
VKIKRTGEML EVRKEELEST LSILMNTTSE VE
//
