Q1LSM8 (SYP_BAUCH) 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:	BCI_0609

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	557 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 – 557	557	Proline--tRNA ligase HAMAP MF_01569		PRO_0000248650

Sequences

	Sequence		Length	Mass (Da)
	Q1LSM8 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 88DC7212658341D5	FASTA	557	62,864
	10 20 30 40 50 60 MRTSQYLLST IKEIPLDAEV ISHQLMLRAG IIRQLASGLY TWLPTGLRIL RKVENIVREE 70 80 90 100 110 120 MNNIGAIEVS MPIVQPANLW LESGRWGQYG PELLRFTDRS TRQFLLGPTH EEVITDLIRN 130 140 150 160 170 180 EVKSYKQLPL NLFQIKTKFR DEVRPRYGVM RSREFIMKDA YSFHTSQQSL QATYDLMYYT 190 200 210 220 230 240 YNTIFNRIGL DVRTVQADPG SIGGHLSHEF LALVSNYEDQ MLLIDASHKA TERNLPSENL 250 260 270 280 290 300 QLVDAPGIYT LTELVKLFNL PIEKIAQIII VHAQQNALYP LVALMVRGDH SINYAQVEKL 310 320 330 340 350 360 PQVASPLVFA TEDEIRLAIG VGSSSLGPIN LPLPLIIDHS VAVMSDFVAG ANIDGKYFFG 370 380 390 400 410 420 INWERDLSLP EVANLTNQNI SVSQPQRLHR TNWIEVGHIF QLGSKYSKVM KATVQGEDGN 430 440 450 460 470 480 NMIMTMGCYG IGITRVVAAA IDKYNDKQGL LLPVSIAPFQ VAIIPINLHK SLLVQTVAEQ 490 500 510 520 530 540 LYNQLSIRKI DVLLDDRKER PGVMFADIEL IGIPHIIIIG DRNLAVQKIE YKNRSNGEKK 550 LMNLSIIVDW IVAKLNS

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000238 Genomic DNA. Translation: ABF13821.1.
RefSeq	YP_589036.1. NC_007984.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LSM8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4056150.
GenomeReviews	Gene locus BCI_0609 in contig CP000238_GR.
KEGG	bci:BCI_0609.
PATRIC	21074723. VBIBauCic75062_0577.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0442.
HOGENOM	HBG403504.
OMA	IQPAELW.
PhylomeDB	Q1LSM8.
Enzyme and pathway databases
BioCyc	BCIC186490:BCI_0609-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.
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_BAUCH

Accession

Primary (citable) accession number: Q1LSM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	May 30, 2006
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program