B0S9Y1 (B0S9Y1_LEPBA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Zn-dependent hydrolase EMBL ABZ94351.1

Gene names

Ordered Locus Names:

LBF_1845

Organism

Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames) [Complete proteome] [HAMAP]

Taxonomic identifier

355278 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid By similarity. SAAS SAAS017782
Catalytic activity	S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate. SAAS SAAS017782
Cofactor	Binds 2 zinc ions per subunit By similarity. SAAS SAAS017782
Subunit structure	Monomer By similarity. SAAS SAAS017782

Ontologies

Keywords
Ligand	Metal-binding SAAS SAAS017782 Zinc SAAS SAAS017782
Molecular function	Hydrolase SAAS SAAS017782 EMBL ABZ94351.1
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	hydroxyacylglutathione hydrolase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	B0S9Y1 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: 0EA720A499D34ECA	FASTA	258	29,541
	10 20 30 40 50 60 MMEVLPIFTN SPLRNYTYLI YSNRTGEVYC VDPYNAPLLL DLMKKMGLKL KGILNTHEHG 70 80 90 100 110 120 DHTEGNLELK EATNCLVYGH TKAKNTIPGL DTTLKEGDIC FSTEGESIEV WDTPGHTFSH 130 140 150 160 170 180 LSFVHKNPNT ILGIFSGDTL FNVGVGNCFR GGDPNTLYET IKNRYATLPD SCLLYPGHDY 190 200 210 220 230 240 WENNLAFSNH VEPNHDFRDR FQKTRTEHFQ STLGLERQLS PFFRLGSGGI KERLTELGES 250 FTDDRSIFLR LRKLRDRW

References

[1]

"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis." Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. , Davies J.K., Medigue C., Adler B. PLoS ONE 3:E1607-E1607(2008) [PubMed: 18270594] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000777 Genomic DNA. Translation: ABZ94351.1.
RefSeq	YP_001962929.1. NC_010842.1.
3D structure databases
ProteinModelPortal	B0S9Y1.
ModBase	Search...
Protein-protein interaction databases
STRING	B0S9Y1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6390036.
GenomeReviews	Gene locus LBF_1845 in contig CP000777_GR.
KEGG	lbf:LBF_1845.
PATRIC	22342801. VBILepBif95142_1955.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG753931.
OMA	QEYAANA.
ProtClustDB	CLSK2336700.
Family and domain databases
InterPro	IPR001279. Beta-lactamas-like. IPR017782. Hydroxyacylglutathione_Hdrlase. [Graphical view]
KO	K01069.
PANTHER	PTHR11935:SF7. PTHR11935:SF7. 1 hit.
Pfam	PF00753. Lactamase_B. 1 hit. [Graphical view]
SMART	SM00849. Lactamase_B. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B0S9Y1_LEPBA

Accession

Primary (citable) accession number: B0S9Y1

Entry history

Integrated into UniProtKB/TrEMBL:	April 8, 2008
Last sequence update:	April 8, 2008
Last modified:	December 14, 2011
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)