SYP_MYCLE
ID SYP_MYCLE Reviewed; 480 AA.
AC Q9Z5I7; Q9CBV1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01571};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01571};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01571};
DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01571};
GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01571}; OrderedLocusNames=ML1553;
GN ORFNames=MLCB596.17c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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_01571}.
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_01571};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01571}.
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC anticodon-binding domain and the C-terminal extension.
CC {ECO:0000255|HAMAP-Rule:MF_01571}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_01571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36573.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL035472; CAB36573.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL583922; CAC30504.1; -; Genomic_DNA.
DR PIR; C87103; C87103.
DR RefSeq; NP_302079.1; NC_002677.1.
DR RefSeq; WP_010908400.1; NC_002677.1.
DR AlphaFoldDB; Q9Z5I7; -.
DR SMR; Q9Z5I7; -.
DR STRING; 272631.ML1553; -.
DR EnsemblBacteria; CAC30504; CAC30504; CAC30504.
DR KEGG; mle:proS; -.
DR PATRIC; fig|272631.5.peg.2930; -.
DR Leproma; ML1553; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_001882_4_2_11; -.
DR OMA; EVYWVTH; -.
DR Proteomes; UP000000806; 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; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 3.30.110.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 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; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR InterPro; IPR017449; Pro-tRNA_synth_II.
DR InterPro; IPR033721; ProRS_core_arch_euk.
DR PANTHER; PTHR43382; PTHR43382; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF09180; ProRS-C_1; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SMART; SM00946; ProRS-C_1; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF64586; SSF64586; 1.
DR TIGRFAMs; TIGR00408; proS_fam_I; 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; Reference proteome.
FT CHAIN 1..480
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000139334"
SQ SEQUENCE 480 AA; 53585 MW; 8DB3E63AA993FD57 CRC64;
MGCNKRGVTR QEDDFSAWYN EVVAKAGLID RGPAKGTMVI RPYGYRIWEL LQDELDSKIK
ELGHENAYFP MLIPENYFNR EAEHVEGFHP ELAVVTHAGG KELSEPLVIR PTSETVIGDM
MAKWITSHRD LPLRLNQWSN VVRWELRPRM LLRTIEFLWQ EGHSAHIEKS DALRETLFAL
DIYTTLARDM AAIPIVSGEK TAGERFAGAL NTYTIEAMMR DGKALQSATT HYLGDNFARA
FNIRYTTAEE QQAFVHTTSF GLSTRMIGAI VMVHGDDKGL VLPPQVAPYQ VVIVPITTGN
KASEVGHAAA DLARRLQAAG VRTHVDARPQ LTPGWKYNEW ELRGVPIRLE LGPRDLEAGT
TVMVRRIGEK AKQPIAIAAA PTELPGILEE FQRTLLERAT QFRDDHTTLV DNWDAFATTV
ATGWALAIHC GNPECEEDIK AETAATPRCV PRQGAPATGR CIRCDAPSAY DKRVIFARAY
