ID D8H813_BACAI Unreviewed; 566 AA.
AC D8H813;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 29-MAY-2013, entry version 22.
DE RecName: Full=Proline--tRNA ligase;
DE EC=6.1.1.15;
DE AltName: Full=Prolyl-tRNA synthetase;
GN Name=proS2; Synonyms=proS; OrderedLocusNames=BACI_c37700;
OS Bacillus cereus var. anthracis (strain CI).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=637380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI;
RX PubMed=20634886; DOI=10.1371/journal.pone.0010986;
RA Klee S.R., Brzuszkiewicz E.B., Nattermann H., Bruggemann H., Dupke S.,
RA Wollherr A., Franz T., Pauli G., Appel B., Liebl W., Couacy-Hymann E.,
RA Boesch C., Meyer F.D., Leendertz F.H., Ellerbrok H., Gottschalk G.,
RA Grunow R., Liesegang H.;
RT "The genome of a Bacillus isolate causing anthrax in chimpanzees
RT combines chromosomal properties of B. cereus with B. anthracis
RT virulence plasmids.";
RL PLoS ONE 5:E10986-E10986(2010).
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; CP001746; ADK06382.1; -; Genomic_DNA.
DR RefSeq; YP_003793520.1; NC_014335.1.
DR EnsemblBacteria; ADK06382; ADK06382; BACI_c37700.
DR GeneID; 9456233; -.
DR KEGG; bal:BACI_c37700; -.
DR PATRIC; 42182356; VBIBacCer111781_4145.
DR HOGENOM; HOG000076894; -.
DR KO; K01881; -.
DR BioCyc; BCER637380:GHO7-3701-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:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:EC.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
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.
SQ SEQUENCE 566 AA; 63139 MW; E153A840BE4C110C CRC64;
MKQSMVFSPT LREVPADAEI KSHQLLLRAG FMRQNASGIY SFLPFGLKVL HKVERIVREE
MERAGAVELL MPAMQAAELW QESGRWYSYG SELMRMKDRN AREFALGATH EEVITDLVRD
EVKSYKKLPL TLYQIQTKFR DEQRPRFGLL RGREFLMKDA YSFHATQESL DEVYDRLYKA
YSNIFARCGL NFRAVIADSG AMGGKDTHEF MVLSDVGEDT IAYSDTSDYA ANIEMAPVVA
TYTKSDEAEK ELEKVATPDQ KAIEEVSAFL NIEADKCIKS MVFKVDEKLV VVLVRGDHEV
NDVKVKNVYG ASVVELASPE EVKELLNCEV GSLGPIGVNG DIEIIADHAV ASIVNGCSGA
NEEGFHYVNV NPERDFKVSQ YTDLRFIQEG DQSPDGNGTI LFARGIEVGH VFKLGTRYSE
AMNATFLDEN GKTQPLIMGC YGIGVSRTVA AIAEQFNDEN GLVWPKAVAP FHVHVIPVNM
KSDAQREMGE NIYNSLQEQG YEVLLDDRAE RAGVKFADAD LFGLPVRVTV GKKADEGIVE
VKVRATGESE EVKVEELQTY IANILK
//
