A5G9I9 (A5G9I9_GEOUR) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Lipoprotein signal peptidase HAMAP-Rule MF_00161
EC=3.4.23.36 HAMAP-Rule MF_00161

Alternative name(s):
Prolipoprotein signal peptidase HAMAP-Rule MF_00161
Signal peptidase II HAMAP-Rule MF_00161

Gene names

Name:	lspA HAMAP-Rule MF_00161
Ordered Locus Names:	Gura_4314

Organism

Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens) [Complete proteome] [HAMAP] EMBL ABQ28457.1

Taxonomic identifier

351605 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter › Geobacter uraniireducens

Protein attributes

Sequence length	163 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This protein specifically catalyzes the removal of signal peptides from prolipoproteins By similarity. RuleBase RU000594 HAMAP-Rule MF_00161 SAAS SAAS001872
Catalytic activity	Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains. RuleBase RU000594 HAMAP-Rule MF_00161 SAAS SAAS001872
Pathway	Protein modification; lipoprotein biosynthesis (signal peptide cleavage). HAMAP-Rule MF_00161 SAAS SAAS001872
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_00161.
Sequence similarities	Belongs to the peptidase A8 family. HAMAP-Rule MF_00161 RuleBase RU004181

Ontologies

Keywords
Cellular component	Cell inner membrane HAMAP-Rule MF_00161 Cell membrane Membrane
Domain	Transmembrane Transmembrane helix HAMAP-Rule MF_00161 SAAS SAAS001872
Molecular function	Aspartyl protease RuleBase RU000594 HAMAP-Rule MF_00161 SAAS SAAS001872 Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Transmembrane	6 – 26	21	Helical; By similarity HAMAP-Rule MF_00161
	Transmembrane	65 – 85	21	Helical; By similarity HAMAP-Rule MF_00161
	Transmembrane	92 – 112	21	Helical; By similarity HAMAP-Rule MF_00161
	Transmembrane	133 – 153	21	Helical; By similarity HAMAP-Rule MF_00161
Sites
	Active site	110	1	By similarity HAMAP-Rule MF_00161
	Active site	137	1	By similarity HAMAP-Rule MF_00161

Sequences

	Sequence		Length	Mass (Da)
	A5G9I9 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: B7F123E40F3EB4E3	FASTA	163	18,583
	10 20 30 40 50 60 MKLKYLILLT VSILVIGIDQ ATKLFVNKVM DLHSSITVVQ NFFNITYMRN KGAAFSFLSN 70 80 90 100 110 120 FNYRIPFFIL VSLVAVVVII SVIYKLRPDQ KFAALSLSLI LSGALGNLID RVRLGEVIDF 130 140 150 160 LDAHWYEHHW PAFNVADSAI CVGVFLLAID MFLEEQRQKK QKD

References

[1]

"Complete sequence of Geobacter uraniireducens Rf4." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M., Lovley D., Richardson P. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Rf4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000698 Genomic DNA. Translation: ABQ28457.1.
RefSeq	YP_001233030.1. NC_009483.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	351605.Gura_4314.
Protein family/group databases
MEROPS	A08.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABQ28457; ABQ28457; Gura_4314.
GeneID	5163373.
KEGG	gur:Gura_4314.
PATRIC	22039094. VBIGeoUra13052_4592.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0597.
HOGENOM	HOG000096992.
KO	K03101.
OMA	ILQGQMW.
ProtClustDB	PRK00376.
Enzyme and pathway databases
BioCyc	GURA351605:GI6A-4371-MONOMER.
UniPathway	UPA00665.
Family and domain databases
HAMAP	MF_00161. LspA.
InterPro	IPR001872. Peptidase_A8. [Graphical view]
Pfam	PF01252. Peptidase_A8. 1 hit. [Graphical view]
PRINTS	PR00781. LIPOSIGPTASE.
TIGRFAMs	TIGR00077. lspA. 1 hit.
PROSITE	PS00855. SPASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A5G9I9_GEOUR

Accession

Primary (citable) accession number: A5G9I9

Entry history

Integrated into UniProtKB/TrEMBL:	June 12, 2007
Last sequence update:	June 12, 2007
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)