ID SYP_BURVG Reviewed; 578 AA.
AC A4JBC2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 43.
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=Bcep1808_0563;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia
OS cepacia (strain R1808)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a
CC two-step reaction: proline is first activated by ATP to form Pro-
CC AMP and then transferred to the acceptor end of tRNA(Pro). As
CC ProRS can inadvertently accommodate and process non-cognate amino
CC acids such as alanine and cysteine, to avoid such errors it has
CC two additional distinct editing activities against alanine. One
CC activity is designated as 'pretransfer' editing and involves the
CC tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other
CC activity is designated 'posttransfer' editing and involves
CC deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-
CC tRNA(Pro) is not edited by ProRS (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
CC diphosphate + L-prolyl-tRNA(Pro).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic
CC domain, the editing domain and the C-terminal anticodon-binding
CC domain (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. ProS type 1 subfamily.
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DR EMBL; CP000614; ABO53575.1; -; Genomic_DNA.
DR RefSeq; YP_001118410.1; NC_009256.1.
DR ProteinModelPortal; A4JBC2; -.
DR STRING; 269482.Bcep1808_0563; -.
DR EnsemblBacteria; ABO53575; ABO53575; Bcep1808_0563.
DR GeneID; 4952257; -.
DR KEGG; bvi:Bcep1808_0563; -.
DR PATRIC; 19319542; VBIBurVie89221_4762.
DR eggNOG; COG0442; -.
DR HOGENOM; HOG000076893; -.
DR KO; K01881; -.
DR OMA; IQPAELW; -.
DR ProtClustDB; PRK09194; -.
DR BioCyc; BVIE269482:GJNA-584-MONOMER; -.
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:HAMAP.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:HAMAP.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:GOC.
DR Gene3D; 3.40.50.800; -; 1.
DR Gene3D; 3.90.960.10; -; 1.
DR HAMAP; MF_01569; Pro_tRNA_synth_type1; 1; -.
DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR004154; Anticodon-bd.
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; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR PANTHER; PTHR11451:SF3; PTHR11451:SF3; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF04073; YbaK; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF52954; Anticodon_bd; 1.
DR SUPFAM; SSF55826; YbaK/aa-tRNA-synth-assoc-reg; 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; Complete proteome; Cytoplasm;
KW Ligase; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1 578 Proline--tRNA ligase.
FT /FTId=PRO_1000069127.
SQ SEQUENCE 578 AA; 63840 MW; 133221698B40EC4A CRC64;
MKASRFFIGT LKEAPADAEI VSHKLMVRAG MIRRVAGGIY NYLPIGLRSI RKVEAIVREE
MNRAGALELL MPAVQPAELW QESGRWEQYG PELLRFKDRK DNDFVIGPTH EEVITDIARN
QIKSYRQMPV NFYQIQTKFR DEIRPRFGVM RGREFLMKDA YSFDKDAAGL NESYRKMYDA
YVRIFTRLGL EFRAVAADSG SIGGNFSHEF HVIADTGEDA IAYCPTSEFA ANIEAAEALP
LIAERAAPAQ AMEKVATPGK AKCEAVAELL AIPLERTIKS IVLATDNEGA EPTIWLVMLR
GDHDLNEIKV SKLPGLKNHR FATEQEIVEW FGTPPGYLGP VGTKKPVKVI ADRTVANMSD
FVVGANEVDY HIAGVNWGRD LPEPDVADVR NVKKGDPSPD GKGVIDICRG IEVGHVFQLG
TKYSEAMGAT FLDESGKPQP MLMGCYGVGV TRILGAAIEQ NFDDKGIIWP ESIAPFELVL
CPMGYDRSEM VREAADKLYA ELTAAGVDVI LDDRGERPGV MFADWELIGV PHRLVIGERG
LKDGKVEYQG RRDAEATLLP ADAAAATVTE KIRAALAH
//
