P57333 (SYP_BUCAI) 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:	BU239

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Acyrthosiphon pisum)

Protein attributes

Sequence length	572 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-Rule MF_01569
Catalytic activity	ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01569
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP-Rule 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 Reference proteome
Gene Ontology (GO)
Biological_process	prolyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP regulation of translational fidelity Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA editing activity Inferred from electronic annotation. Source: InterPro proline-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 572	572	Proline--tRNA ligase HAMAP-Rule MF_01569		PRO_0000139322

Sequences

	Sequence		Length	Mass (Da)
	P57333 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 44B4BF1A73F16E68	FASTA	572	66,325
	10 20 30 40 50 60 MLTSQYLLST SKDIPYDAKI ISHQLMIRSG MIRKTSSGLY VWLPTGMRVL KKIKNIITTE 70 80 90 100 110 120 MEKINALEIL MPIIQPEYLW KESRRLNLYG EELLRFLDRR KNQFILGPTN EEVVTNFIGS 130 140 150 160 170 180 EIHSYKQLPL TVYQIQTKFR DEIRPRFGII RTREFTMKDA YSFHINQSCL ENTYNKFYDS 190 200 210 220 230 240 YINIFKKMNL NFCAVKADSG SMGGNISHEF QAFSQNGEDE IVFSNDKLYS SNMNMAESIE 250 260 270 280 290 300 TIDFFKKKYS SCLIKNKTNT KKSIIMSEKL NTPLINQIQT FLIQTKINDI TSIAALLIRG 310 320 330 340 350 360 DHELNFFKVE KIDIINKPLV FLNEKEVISL IGVKKEFLGP LGLKVPIIAD ISTFNMKNFT 370 380 390 400 410 420 IGSNINKHFF INVNWNIDLP MPIFKDIRKV TKNDLSPNGS GYLNIKQSIE IGHIFQLGQK 430 440 450 460 470 480 YSRKIQQSVK IKNGNLKNLY MGCYGIGITR IAAAVIEQHH DKNGIIWPDS IAPFEVVILP 490 500 510 520 530 540 INMKKDNKIK IIAHFLYKKF KKTGIDVILD DRDERPGVMF NEVDLIGIPH QIIISKRSIN 550 560 570 YDNVEYRERK NKENILINIK DIKNFIIQKL KK

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12954.1.
RefSeq	NP_240068.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57333.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB12954; BAB12954; BAB12954.
GeneID	1109682.
KEGG	buc:BU239.
PATRIC	21244000. VBIBucAph127364_0252.
Phylogenomic databases
eggNOG	COG0442.
HOGENOM	HOG000076893.
KO	K01881.
OMA	IQPAELW.
ProtClustDB	PRK09194.
Family and domain databases
Gene3D	3.40.50.800. 1 hit. 3.90.960.10. 1 hit.
HAMAP	MF_01569. Pro_tRNA_synth_type1.
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR002316. Pro-tRNA-ligase_IIa. IPR004500. Pro-tRNA-synth_IIa_bac-type. IPR023717. Pro-tRNA-Synthase_IIa_type1. IPR007214. YbaK/aa-tRNA-synth-assoc-dom. [Graphical view]
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_BUCAI

Accession

Primary (citable) accession number: P57333

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program