Q8FP97 (SYP_COREF) 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:	CE1888

Organism

Corynebacterium efficiens [Complete proteome] [HAMAP]

Taxonomic identifier

152794 [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
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_0000248677

Sequences

	Sequence		Length	Mass (Da)
	Q8FP97 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: FD14582D710CB6C0	FASTA	588	64,662
	10 20 30 40 50 60 MITRLSTLFL RTLREDPADA EVPSHKLLVR AGYIRRVAPG VYSWLPLGLR ALRNIEQVVR 70 80 90 100 110 120 EEMDAIGGQE LLFPGLLPRE PYETTQRWTE YGDSLFRLKD RKGADYLLGP THEEMFASTV 130 140 150 160 170 180 KDLYSSYKDF PVTLYQIQTK YRDEERPRAG ILRGREFVMK DSYSFDMTDA GLEESYARHR 190 200 210 220 230 240 AAYQRIFDRL GIEYVICKAT SGAMGGSASE EFLAVSANGE DTFVRATDGD FAANVEAVVT 250 260 270 280 290 300 QPGQERPIEG LPEAVVHETP VSETIETLVA WANSIGVTVD GREVQASDTL KCIVVKTREP 310 320 330 340 350 360 GAEEWELTGV LVPGDREVDM KRLEASLEPA EVELAVEADF AKYPFLVKGY VGPVGLARNG 370 380 390 400 410 420 VRVLADPRVV TGTSWITGAD EKERHVVGLV AGRDFTPDGF IEAAEIREGD PAPEGQGTLT 430 440 450 460 470 480 LARGIEIGHI FQLGRKYTEA FDVQILDENG KRAIPTMGSY GIGVSRLLAV LAEQRHDEAG 490 500 510 520 530 540 LNWSPAVAPY QVHVVAANKD AAAIEAAERY ATELSQAGID VLFDDRPKVS PGVKFKDAEL 550 560 570 580 LGMPFALILG RGYADGTVEL RVRGGEKTEL PVDEAVETIV RLVNEARG

References

[1]

"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens." Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T. Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000035 Genomic DNA. Translation: BAC18698.1.
RefSeq	NP_738498.1. NC_004369.1.
3D structure databases
ProteinModelPortal	Q8FP97.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1034582.
GenomeReviews	Gene locus CE1888 in contig BA000035_GR.
KEGG	cef:CE1888.
NMPDR	fig|196164.1.peg.1888.
PATRIC	21489925. VBICorEff9312_1876.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG403504.
OMA	IQPAELW.
PhylomeDB	Q8FP97.
ProtClustDB	PRK09194.
Enzyme and pathway databases
BioCyc	CEFF196164:CE1888-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_COREF

Accession

Primary (citable) accession number: Q8FP97

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program