Q8NP31 (SYP_CORGL) 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:	Cgl1994, cg2185

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	588 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 Reference 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 – 588	588	Proline--tRNA ligase HAMAP MF_01569		PRO_0000248678

Sequences

	Sequence		Length	Mass (Da)
	Q8NP31 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 8F551DB79DA142FF	FASTA	588	64,332
	10 20 30 40 50 60 MITRLSTLFL RTLREDPADA EVPSHKLLVR AGYIRRVAPG IYSWLPLGLR AVRNIEAVVR 70 80 90 100 110 120 EEMDAIGGQE LLFPALLPRE PYETTQRWTE YGDSLFRLKD RKGADYLLGP THEEMFAATV 130 140 150 160 170 180 KDLYNSYKDF PVTLYQIQTK YRDEERPRAG VLRGREFVMK DSYSFDISDA GLDESYAKHR 190 200 210 220 230 240 AAYQRIFDRL GLEYAICQAT SGAMGGSASE EFLAVSENGE DTFVRSTSGN YAANVEAVVT 250 260 270 280 290 300 QPGVERDIEG LPEAVTYETP VSETIDALVD WANSIDVQIE GREVTAADTL KCIVVKVREP 310 320 330 340 350 360 GAEEAELTGI LLPGDREVDM KRLEASLEPA EVELAVESDF ADNPFLVKGY VGPVGLAKNG 370 380 390 400 410 420 VKVLADPRVV TGTSWITGAD EKERHVVGLV AGRDFTPDGF IEAAEIKEGD PAPAGEGTLT 430 440 450 460 470 480 LARGIEIGHI FQLGRKYTEA FDVQILDENG KRAIPTMGSY GLGVTRLLAV LAEQRHDDAG 490 500 510 520 530 540 LNWSVEVAPY QVHVVAANKD AAAIEAAERF AAELSAAGLD VLFDDRPKVS PGVKFKDAEL 550 560 570 580 LGMPFALILG RGYAEGKVEL RVRGGEKSEL DADQAVAQIV EMVAQARN

References

[1]

"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

[2]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB99387.1. BX927153 Genomic DNA. Translation: CAF20335.1.
RefSeq	NP_601200.1. NC_003450.3. YP_226236.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NP31.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1019951. 3344363.
GenomeReviews	Gene locus Cgl1994 in contig BA000036_GR. Gene locus cg2185 in contig BX927147_GR.
KEGG	cgb:cg2185. cgl:NCgl1919.
PATRIC	21495994. VBICorGlu203724_1933.
Phylogenomic databases
HOGENOM	HBG403504.
OMA	IQPAELW.
PhylomeDB	Q8NP31.
ProtClustDB	PRK09194.
Enzyme and pathway databases
BioCyc	CGLU196627:CG2185-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_CORGL

Accession

Primary (citable) accession number: Q8NP31
Secondary accession number(s): Q6M447

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program