Reviewed, UniProtKB/Swiss-Prot A8FDC1 (SYP_BACP2)

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:	BPUM_1556

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]

Taxonomic identifier

315750 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	565 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 – 565	565	Prolyl-tRNA synthetase HAMAP MF_01569		PRO_1000069121

Sequences

	Sequence		Length	Mass (Da)
	A8FDC1-1 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: 2FFAC17B680681E5	FASTA	565	63,357
	10 20 30 40 50 60 MRQSLTFIPT LREVPADAEA KSHQLLVRAG FIRQNTSGIY HYLPLAHKVI QHIQSIVRKE 70 80 90 100 110 120 MEKAGAAELL MPVLQQAEMW QESGRWYTYG PELMRMKDRH GREFALGPTH EEVITSLVRS 130 140 150 160 170 180 EVKSYKKLPL TLYQIQSKFR DEQRPRFGLL RGREFIMKDA YSFHSSPESL DDTYNKMFTA 190 200 210 220 230 240 YSNVFSKVGL NFRPVIADSG AMGGKDTHEF MALSEVGEDT IAYSDTSSYA ANIEMAEAVY 250 260 270 280 290 300 QGEEANPADF KELEKVHTPQ VKTIQDIAGF LDVDPSLCIK SVLFKADDAY VLILTRGDHE 310 320 330 340 350 360 VNDVKVKNLV GAQLVELATR EEVLEVIGTE PGFVGPVKLE AEVDIYADLT VKGMTNAVAG 370 380 390 400 410 420 ANEADYHYVN VNPARDVSVK EFTDLRFIQE GDVSPDGEGT IQFAKGIEVG QVFKLGTRYS 430 440 450 460 470 480 ESMDATYLDE NGRAQPMIMG CYGIGISRTL SAIVEQHHDE KGIIWPEAVA PYDLHLLALN 490 500 510 520 530 540 MKNDAQKELA ETLYERLENE GFDVLFDDRQ ERAGVKFADS DLIGLPIRIS CGKRSEEGIV 550 560 EVKFRKSGES HEVSVDELIS FIRQA

References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. , Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., Weinstock G.M. PLoS ONE 2:E928-E928(2007) [PubMed: 17895969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000813 Genomic DNA. Translation: ABV62238.1.
RefSeq	YP_001486798.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A8FDC1.
Genome annotation databases
GeneID	5620823.
GenomeReviews	Gene locus BPUM_1556 in contig CP000813_GR.
KEGG	bpu:BPUM_1556.
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

SYP_BACP2

Accession

Primary (citable) accession number: A8FDC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 13, 2007
Last modified:	November 3, 2009
This is version 15 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)