Q6FE23 (SYP_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proline--tRNA ligase
EC=6.1.1.15

Alternative name(s):
Prolyl-tRNA synthetase
Short name=ProRS

Gene names

Name:	proS
Ordered Locus Names:	ACIAD0782

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
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. HAMAP MF_01569
Catalytic activity	ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01569
Subunit structure	Homodimer By similarity. HAMAP MF_01569
Subcellular location	Cytoplasm By similarity HAMAP MF_01569.
Domain	Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP MF_01569
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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW proline-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 570	570	Proline--tRNA ligase HAMAP MF_01569		PRO_0000248637

Sequences

	Sequence		Length	Mass (Da)
	Q6FE23 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: FA7306BFF0DC50C7	FASTA	570	63,002
	10 20 30 40 50 60 MRASRFLFAT LRETPNDAEV ISHQLMLRAG MIRKLASGLY TWLPMGVRVL NKVEAIVREE 70 80 90 100 110 120 MNRSGALEVF MPVTQPASLW EESGRYVQYG PELLRFKDRH DNPFVLGPTH EEVITDLARN 130 140 150 160 170 180 ELKSYKQLPI NFYQIQTKFR DEIRPRFGVM RSREFIMKDA YSFHVDQASL QETYDNMYDT 190 200 210 220 230 240 YCRIFTRLGL DFRPVQADTG SIGGSGSHEF HVLADSGEDD IVFSTESDYA ANVEKAEAVL 250 260 270 280 290 300 VGERAAPAQA LSIVDTPNQK TIADVCTFLN ADPKQSVKAL LVQGNADEKG NVPVIALFLR 310 320 330 340 350 360 GDHELNEIKA EHHPLIAAPL TFATEAQLQE LGLTAGYVGP QGLVEKGLTV IVDRAASVLS 370 380 390 400 410 420 DFIAGANEAD KHATGVNWER DAKFSEIYDL RNVVDGDPSP DGQGVLQIKR GIEVGHIFQL 430 440 450 460 470 480 GQKYSEALNC TVLGDDGKPL VVTMGCYGIG VTRVVASAIE QNYDDKGIIW PSAIAPFEIA 490 500 510 520 530 540 IVPMNAHKSP KTLEAAEALY AELQAQGYDV LLDDRNERPG VKFSDLELTG IPHRIVIGEK 550 560 570 GLDAGTFEYK GRTDAESVNL TKDELLAKLK

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ADP1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG67685.1.
RefSeq	YP_045507.1. NC_005966.1.
3D structure databases
ProteinModelPortal	Q6FE23.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FE23.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2880049.
GenomeReviews	Gene locus ACIAD0782 in contig CR543861_GR.
KEGG	aci:ACIAD0782.
NMPDR	fig|62977.3.peg.640.
PATRIC	20739452. VBIAciSp98416_0696.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0442.
HOGENOM	HBG403504.
OMA	IQPAELW.
PhylomeDB	Q6FE23.
ProtClustDB	PRK09194.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD0782-MONOMER.
Family and domain databases
HAMAP	MF_01569. Pro_tRNA_synth_type1. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR002316. Pro-tRNA-synth_IIa. IPR004500. Pro-tRNA-synth_IIa_bac-type. IPR023717. Pro-tRNA-Synthase_IIa_type1. IPR007214. YbaK/aa-tRNA-synth-assoc-dom. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit. G3DSA:3.90.960.10. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
KO	K01881.
PANTHER	PTHR11451:SF3. PTHR11451:SF3. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF04073. YbaK. 1 hit. [Graphical view]
PRINTS	PR01046. TRNASYNTHPRO.
SUPFAM	SSF52954. Anticodon_bd. 1 hit. SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
TIGRFAMs	TIGR00409. ProS_fam_II. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYP_ACIAD

Accession

Primary (citable) accession number: Q6FE23

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program