Reviewed, UniProtKB/Swiss-Prot Q83F67 (SYP_COXBU)

Names and origin

Protein names

Recommended name:
    Prolyl-tRNA synthetase
    EC=6.1.1.15
Alternative name(s):
    Proline--tRNA ligase
      Short name=ProRS

Gene names

Name:	proS
Ordered Locus Names:	CBU_0081

Organism

Coxiella burnetii [Complete proteome] [HAMAP]

Taxonomic identifier

777 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS By similarity.
Catalytic activity	ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).
Subunit structure	Homodimer By similarity.
Subcellular location	CytoplasmBy similarity.
Domain	Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	prolyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP proline-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 566	566	Prolyl-tRNA synthetase

Sequences

	Sequence		Length	Mass (Da)
	Q83F67-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 46EAB65336DC0383	FASTA	566	63,589
	10 20 30 40 50 60 MLMKVSQFFL ATVKETPADA VLASHQLMIR AGMLRKLASG LYTWLPLGLR VLQKVADVVR 70 80 90 100 110 120 EEMNRAGALE LLMPIVQPAS LWQESGRWEA YGAELLRIMD RHQNGFCFGP THEEVITDIA 130 140 150 160 170 180 RQELKSYKQL PLNFYQIQTK FRDEIRPRFG VMRSREFLMK DAYSFDLDEK GMQAAYEKMF 190 200 210 220 230 240 DAYRRIFTRL GLNFRAVLAD TGAIGGDYSH EFQVLADVGE DTVVYSDESD YAANIEKAAA 250 260 270 280 290 300 QAPQGERVKP VAEMKKIATP GVRTIKQLAD KANILPEKGV KTLIVKGDES SLIALILRGD 310 320 330 340 350 360 HELNDVKAQH LPGVAFPLQF ADEKEIREAI GCGPGSLGPV NLPIPFIVDR DAAQLVDFSC 370 380 390 400 410 420 GANEDDFHWI NVNWERDVPL GSVADIRKVV EGDISPDGKG RLRFARGIEV GQVFQLGDKY 430 440 450 460 470 480 SRKMNATVVD ELGKSRYLQM GCYGIGVSRT VAAAIEQNHD ERGIIWPMPM APFFIALVPV 490 500 510 520 530 540 NMHKSYRVRE ACEKLYNELI DAGYEVLWDD RKERPGVMFA DMDLIGIPHR LVISESGLDR 550 560 GIVEYKARKS KEAENVSLEN VLSVFR

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016828 Genomic DNA. Translation: AAO89648.1.
RefSeq	NP_819134.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1207951.
GenomeReviews	Gene locus CBU_0081 in contig AE016828_GR.
KEGG	cbu:CBU_0081.
NMPDR	fig|227377.1.peg.78.
TIGR	CBU_0081.
Phylogenomic databases
HOGENOM	Q83F67.
Enzyme and pathway databases
BioCyc	CBUR227377:CBU_0081-MON.
Family and domain databases
HAMAP	MF_01569. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon_bd. IPR002316. Pro-tRNA-synth_IIa. IPR004500. Pro-tRNA-synth_IIa_bac. IPR007214. YbaK/aa-tRNA-synth-assoc-reg. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF04073. YbaK. 1 hit. [Graphical view]
PRINTS	PR01046. TRNASYNTHPRO.
TIGRFAMs	TIGR00409. proS_fam_II. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProDom	Q83F67. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

SYP_COXBU

Accession

Primary (citable) accession number: Q83F67

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	June 1, 2003
Last modified:	July 22, 2008
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)