SYP_AQUAE
ID SYP_AQUAE Reviewed; 570 AA.
AC O66690;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Proline--tRNA ligase;
DE EC=6.1.1.15;
DE AltName: Full=Prolyl-tRNA synthetase;
DE Short=ProRS;
GN Name=proS; OrderedLocusNames=aq_365;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP PROLINE AND CYSTEINE ACTIVATION, POSTTRANSFER EDITING ACTIVITY, AND KINETIC
RP PARAMETERS.
RX PubMed=12130657; DOI=10.1074/jbc.m206928200;
RA Ahel I., Stathopoulos C., Ambrogelly A., Sauerwald A., Toogood H.,
RA Hartsch T., Soell D.;
RT "Cysteine activation is an inherent in vitro property of prolyl-tRNA
RT synthetases.";
RL J. Biol. Chem. 277:34743-34748(2002).
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 -!- 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;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for proline (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:12130657};
CC KM=0.05 mM for cysteine (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:12130657};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC editing domain and the C-terminal anticodon-binding domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 1 subfamily. {ECO:0000305}.
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DR EMBL; AE000657; AAC06648.1; -; Genomic_DNA.
DR PIR; F70332; F70332.
DR RefSeq; NP_213250.1; NC_000918.1.
DR RefSeq; WP_010880188.1; NC_000918.1.
DR AlphaFoldDB; O66690; -.
DR SMR; O66690; -.
DR STRING; 224324.aq_365; -.
DR PRIDE; O66690; -.
DR EnsemblBacteria; AAC06648; AAC06648; aq_365.
DR KEGG; aae:aq_365; -.
DR PATRIC; fig|224324.8.peg.295; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_016739_0_0_0; -.
DR InParanoid; O66690; -.
DR OMA; NCDYAAN; -.
DR OrthoDB; 665824at2; -.
DR SABIO-RK; O66690; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..570
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000248226"
SQ SEQUENCE 570 AA; 65873 MW; 6B12F0FA016DAE14 CRC64;
MRWSRYFLYT EKEEPKEAEA PSHRLLLKAG FIKQVSAGIY ELLPPAYKVL KKVESIIRKE
MDRSGAQELL LTVLNPKELW EETGRWETYG EELFKLKDRN GREYCLGPTH EEEITDLVRR
VVRSYRQLPV ILYQIQVKFR DEKRPRFGLI RAREFIMKDA YSFDTDDMSA MISYEAMKFA
YQRIFNKLRL NVIMAEADVG QIGGKMSHEF IAFTDYGEAK VAYCENCGYA ANAEIVPLPK
PEEEKEEEKP MEKVHTPNVH TIEELSKFLD VHPSKIMKAV LYIVNEKEPV LVLIRGDREI
DENKLEKVLG TDNFRLATDE EVQELLGTKK GFIGIFNLPE NIKVLWDNSL YGVKNLVVAL
NEPDWHYINV NPGRDFQYGE FVDVAEVREG DPCPKCGSPL KVRRGLELGH IFLLGTRYSE
PMKAYFTDRD GKEKPIIMGC YGIGVSRILA ALVEQYHDDK GIKWPTPVAP FELDIILLNT
KDEEMKNVAE KLYLEAEEKG IDVIFDDREE SPGFKFADAD LVGFPYRIVV GKKVKEGKVE
VQSRHTGEKW DVEIEKAIDF VKEKIEEDKK
