Q732Q0 (SYP1_BACC1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proline--tRNA ligase 1
EC=6.1.1.15

Alternative name(s):
Prolyl-tRNA synthetase 1
Short name=ProRS 1

Gene names

Name:	proS1
Ordered Locus Names:	BCE_3860

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus cereus

Protein attributes

Sequence length	566 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
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 – 566	566	Proline--tRNA ligase 1 HAMAP-Rule MF_01569		PRO_0000248643

Sequences

	Sequence		Length	Mass (Da)
	Q732Q0 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 16D1F26FF6452B02	FASTA	566	63,122
	10 20 30 40 50 60 MKQSMVFSPT LREVPADAEI KSHQLLLRAG FMRQNASGIY SFLPFGLKVL HKVERIVREE 70 80 90 100 110 120 MERAGAVELL MPAMQAAELW QESGRWYSYG SELMRMKDRN AREFALGATH EEVITDLVRD 130 140 150 160 170 180 EVKSYKKLPL TLYQIQTKFR DEQRPRFGLL RGREFLMKDA YSFHATQESL DEVYDRLYKA 190 200 210 220 230 240 YSNIFARCGL NFRAVIADSG AMGGKDTHEF MVLSDVGEDT IAYSDTSDYA ANIEMAPVVA 250 260 270 280 290 300 TYTKSDEAEK ALEKVATPDQ KAIEEVSAFL NIEAEKCIKS MVFKVDEKLV VVLVRGDHEV 310 320 330 340 350 360 NDVKVKNVYG ASVVELASHE EVKELLNCEV GSLGPIGVTG DIEIIADHAV ASIVNGCSGA 370 380 390 400 410 420 NEEGFHYVNV NPERDFKVSQ YTDLRFIQEG DQSPDGNGTI LFARGIEVGH VFKLGTRYSE 430 440 450 460 470 480 AMNATFLDEN GKTQPLIMGC YGIGVSRTVA AIAEQFNDEN GLVWPKAVAP FHVHVIPVNM 490 500 510 520 530 540 KSDAQREMGE NIYNSLQEQG YEVLLDDRAE RAGVKFADAD LFGLPVRVTV GKKADEGIVE 550 560 VKVRATGESE EVKVEELQTY IANILK

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017194 Genomic DNA. Translation: AAS42765.1.
RefSeq	NP_980157.1. NC_003909.8.
3D structure databases
ProteinModelPortal	Q732Q0.
SMR	Q732Q0. Positions 1-565.
ModBase	Search...
Protein-protein interaction databases
STRING	222523.BCE_3860.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAS42765; AAS42765; BCE_3860.
GeneID	2749973.
KEGG	bca:BCE_3860.
PATRIC	18856376. VBIBacCer118379_3687.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0442.
HOGENOM	HOG000076894.
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

SYP1_BACC1

Accession

Primary (citable) accession number: Q732Q0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program