Reviewed, UniProtKB/Swiss-Prot A0RHJ2 (SYP1_BACAH)

Names and origin

Protein names

Recommended name:
    Prolyl-tRNA synthetase 1
    EC=6.1.1.15
Alternative name(s):
    Proline--tRNA ligase 1
      Short name=ProRS 1

Gene names

Name:	proS1
Ordered Locus Names:	BALH_3449

Organism

Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]

Taxonomic identifier

412694 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP 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.
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
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP 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	Prolyl-tRNA synthetase 1 HAMAP MF_01569		PRO_0000288312

Sequences

	Sequence		Length	Mass (Da)
	A0RHJ2-1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 5953A84E3E4C1108	FASTA	566	63,179
	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 ELEKVATPDQ KAIEEVSAFL NIEADKCIKS MVFKVDEKLV VVLVRGDHEV 310 320 330 340 350 360 NDVKVKNVYG ASVVELASHE EVKELLNCEV GSLGPIGVNG 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 complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S. , Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S. J. Bacteriol. 189:3680-3681(2007) [PubMed: 17337577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000485 Genomic DNA. Translation: ABK86685.1.
RefSeq	YP_896192.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A0RHJ2.
Genome annotation databases
GeneID	4545099.
GenomeReviews	Gene locus BALH_3449 in contig CP000485_GR.
KEGG	btl:BALH_3449.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	VVSHQLM.
Family and domain databases
HAMAP	MF_01569. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004154. Anticodon_bd. IPR004500. Pro-tRNA-synth_IIa_bac. IPR002316. Pro-tRNA-synth_IIa_cons-reg. IPR007214. YbaK/aa-tRNA-synth-assoc-reg. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF04073. YbaK. 1 hit. [Graphical view]
PRINTS	PR01046. TRNASYNTHPRO.
TIGRFAMs	TIGR00409. proS_fam_II. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYP1_BACAH

Accession

Primary (citable) accession number: A0RHJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	January 9, 2007
Last modified:	November 3, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)