Reviewed, UniProtKB/Swiss-Prot Q1IST4 (SYP_ACIBL)

Names and origin

Protein names

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

Gene names

Name:	proS
Ordered Locus Names:	Acid345_1063

Organism

Acidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Candidatus Koribacter

Protein attributes

Sequence length	587 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 – 587	587	Prolyl-tRNA synthetase HAMAP MF_01569		PRO_0000288302

Sequences

	Sequence		Length	Mass (Da)
	Q1IST4-1 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 8F1044DE10758567	FASTA	587	65,205
	10 20 30 40 50 60 MHRWSKLFIP TLREAPADAE VASHKFLVRA GYIRQLAAGI YSYLFLGNRS MNKIIGIVRE 70 80 90 100 110 120 EMDKIGQEYY LPALNPREIW EASGRWAVMG DNMFRLKDRK GAELCLGMTH EEIMTEIARK 130 140 150 160 170 180 ELRSYKQLPQ IWYQIQTKFR DEPRPRSGLL RVRQFIMKDS YSFDIDAAGL DISYQKHHDA 190 200 210 220 230 240 YCRIFDRCGL KYVVVHADSG AMGGSGSQEF MVYTDAGEDL VASCANCSYA ANVEKATSKL 250 260 270 280 290 300 EAIEDLVATA DTPELVHTPG QKTIEQVAAY LGVSPKNKIK TLAYMMAAPK GAKDGREQAL 310 320 330 340 350 360 VVLLRGDHML NEAKLGAAIK GREVRPMTEE EIQDLFHSPA GYLGPLNVEW AKTSEDTEKP 370 380 390 400 410 420 LLLLDEALVS RKNLIAGANK EEYHVRNLTP GESFQFTGSA DLRMVAEGEP CPNCGHALKV 430 440 450 460 470 480 GKTVEIGHIF KLGYKYTDAM GARVLDKDGK EVMPIMGSYG IGMERILTAS VEQSNDDNGF 490 500 510 520 530 540 WLPAQIAPFE VVVTPTNVSD EKLAKGAEEI AAKLEAAGFD VILDDRDERP GVKFKDADLV 550 560 570 580 GIPVRINVGK KFVEGKVEVI HRSTRESLDA TIPEIVEKIA AWLKPSA

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000360 Genomic DNA. Translation: ABF40066.1.
RefSeq	YP_590140.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IST4.
Genome annotation databases
GeneID	4068712.
GenomeReviews	Gene locus Acid345_1063 in contig CP000360_GR.
KEGG	aba:Acid345_1063.
NMPDR	fig|204669.6.peg.1050.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1IST4.
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

SYP_ACIBL

Accession

Primary (citable) accession number: Q1IST4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	June 13, 2006
Last modified:	November 3, 2009
This is version 24 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)