ID   SYP_BAUCH               Reviewed;         557 AA.
AC   Q1LSM8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Prolyl-tRNA synthetase;
DE            EC=6.1.1.15;
DE   AltName: Full=Proline--tRNA ligase;
DE            Short=ProRS;
GN   Name=proS; OrderedLocusNames=BCI_0609;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF13821.1; -; Genomic_DNA.
DR   RefSeq; YP_589036.1; -.
DR   GeneID; 4056150; -.
DR   GenomeReviews; CP000238_GR; BCI_0609.
DR   KEGG; bci:BCI_0609; -.
DR   HOGENOM; Q1LSM8; -.
DR   OMA; Q1LSM8; VVSHQLM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   HAMAP; MF_01569; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004154; Anticodon_bd.
DR   InterPro; IPR004500; Pro-tRNA-synth_IIa_bac.
DR   InterPro; IPR002316; Pro-tRNA-synth_IIa_cons-reg.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-reg.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF04073; YbaK; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
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    557       Prolyl-tRNA synthetase.
FT                                /FTId=PRO_0000248650.
SQ   SEQUENCE   557 AA;  62864 MW;  88DC7212658341D5 CRC64;
     MRTSQYLLST IKEIPLDAEV ISHQLMLRAG IIRQLASGLY TWLPTGLRIL RKVENIVREE
     MNNIGAIEVS MPIVQPANLW LESGRWGQYG PELLRFTDRS TRQFLLGPTH EEVITDLIRN
     EVKSYKQLPL NLFQIKTKFR DEVRPRYGVM RSREFIMKDA YSFHTSQQSL QATYDLMYYT
     YNTIFNRIGL DVRTVQADPG SIGGHLSHEF LALVSNYEDQ MLLIDASHKA TERNLPSENL
     QLVDAPGIYT LTELVKLFNL PIEKIAQIII VHAQQNALYP LVALMVRGDH SINYAQVEKL
     PQVASPLVFA TEDEIRLAIG VGSSSLGPIN LPLPLIIDHS VAVMSDFVAG ANIDGKYFFG
     INWERDLSLP EVANLTNQNI SVSQPQRLHR TNWIEVGHIF QLGSKYSKVM KATVQGEDGN
     NMIMTMGCYG IGITRVVAAA IDKYNDKQGL LLPVSIAPFQ VAIIPINLHK SLLVQTVAEQ
     LYNQLSIRKI DVLLDDRKER PGVMFADIEL IGIPHIIIIG DRNLAVQKIE YKNRSNGEKK
     LMNLSIIVDW IVAKLNS
//