Proline--tRNA ligase - Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700)

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Q3JZ37 (SYP_STRA1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	SAK_1871

Organism

Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700) [Complete proteome] [HAMAP]

Taxonomic identifier

205921 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length	617 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.
Sequence caution	The sequence ABA46079.1 differs from that shown. Reason: Erroneous initiation.

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 – 617

617

Proline--tRNA ligase HAMAP-Rule MF_01569

PRO_0000248773

Sequences

Sequence

Length

Mass (Da)

Tools

Q3JZ37 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: B7479B2B60BE9F44
Show »

FASTA

617

68,997

        10         20         30         40         50         60 
MKQSKMLIPT LREMPSDAQV ISHALMVRAG YVRQVSAGIY AYLPLANRTI EKFKTIMRQE 

        70         80         90        100        110        120 
FEKIGAVEML APALLTADLW RESGRYETYG EDLYKLKNRD QSDFILGPTH EETFTTLVRD 

       130        140        150        160        170        180 
AVKSYKQLPL NLYQIQSKYR DEKRPRNGLL RTREFIMKDG YSFHKDYEDL DVTYEDYRKA 

       190        200        210        220        230        240 
YEAIFTRAGL DFKGIIGDGG AMGGKDSQEF MAVTPNRTDL NRWLVLDKTI PSIDDIPEDV 

       250        260        270        280        290        300 
LEEIKAELSA WLVSGEDTIA YSTESSYAAN LEMATNEYKP STKAATFEEV TKVETPNCKS 

       310        320        330        340        350        360 
IDEVAGFLSI DKNQTIKTLL FIADEQPVVA LLVGNDQVND VKLKNYLAAD FLEPASEEQA 

       370        380        390        400        410        420 
KEIFGAGFGS LGPVNLPESV KIIADRKVQD LANAVSGANQ DGYHFTGVNP ERDFTAEYVD 

       430        440        450        460        470        480 
IREVKEGEIS PDGKGTLKFS RGIEIGHIFK LGTRYSDSMG ANILDENGRS NPIVMGCYGI 

       490        500        510        520        530        540 
GVSRILSAVI EQHARLFVNK TPKGAYRFAW GINFPEELAP FDVHLITVNV KDQESQDLTE 

       550        560        570        580        590        600 
KIEADLMLKG YEVLTDDRNE RVGSKFSDSD LIGLPIRVTV GKKASEGIVE VKIKASGDTI 

       610 
EVHADNLIET LEILTKK

« Hide

References

[1]

"Genome analysis of multiple pathogenic isolates of Streptococcus agalactiae: implications for the microbial 'pan-genome'."
Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D., Hauser C.R., Sundaram J.P.

Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27591 / A909 / CDC SS700.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000114 Genomic DNA. Translation: ABA46079.1. Different initiation.
RefSeq	YP_330466.2. NC_007432.1.
3D structure databases
ProteinModelPortal	Q3JZ37.
SMR	Q3JZ37. Positions 1-614.
ModBase	Search...
Protein-protein interaction databases
STRING	205921.SAK_1871.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABA46079; ABA46079; SAK_1871.
GeneID	3686797.
KEGG	sak:SAK_1871.
PATRIC	19635076. VBIStrAga82541_1841.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0442.
HOGENOM	HOG000076893.
KO	K01881.
ProtClustDB	PRK09194.
Enzyme and pathway databases
BioCyc	SAGA205921:GHD7-1877-MONOMER.
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. 2 hits.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYP_STRA1

Accession

Primary (citable) accession number: Q3JZ37

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents