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Protein

Metalloprotease LoiP

Gene

loiP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB.4 Publications

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Zinc; catalyticSequence analysis
Active sitei131 – 1311Sequence analysis
Metal bindingi134 – 1341Zinc; catalyticSequence analysis
Metal bindingi189 – 1891Zinc; catalyticBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: InterPro
  • metallopeptidase activity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Stress response

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG11291-MONOMER.
ECOL316407:JW2903-MONOMER.
MetaCyc:EG11291-MONOMER.

Protein family/group databases

MEROPSiM48.A04.

Names & Taxonomyi

Protein namesi
Recommended name:
Metalloprotease LoiP (EC:3.4.24.-)
Gene namesi
Name:loiP
Synonyms:yggG
Ordered Locus Names:b2936, JW2903
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11291. loiP.

Subcellular locationi

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818PROSITE-ProRule annotationAdd
BLAST
Chaini19 – 252234Metalloprotease LoiPPRO_0000138938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi19 – 191N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi19 – 191S-diacylglycerol cysteinePROSITE-ProRule annotation
Disulfide bondi53 ↔ 1081 Publication

Post-translational modificationi

The intramolecular disulfide bond improves the stability and the activity of LoiP. It forms even in the absence of the oxido-reductase DsbA (PubMed:22491786).1 Publication

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate

Proteomic databases

EPDiP25894.
PaxDbiP25894.
PRIDEiP25894.

Expressioni

Inductioni

Induced by heat shock and low osmolarity.3 Publications

Interactioni

Subunit structurei

Interacts with Era and BepA.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ydiBP0A6D51EBI-560654,EBI-560638

Protein-protein interaction databases

BioGridi4263066. 14 interactions.
DIPiDIP-12186N.
IntActiP25894. 3 interactions.
MINTiMINT-1288575.
STRINGi511145.b2936.

Structurei

3D structure databases

ProteinModelPortaliP25894.
SMRiP25894. Positions 91-247.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M48B family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108K0D. Bacteria.
COG0501. LUCA.
HOGENOMiHOG000264551.
InParanoidiP25894.
KOiK07387.
OMAiMFDSHPG.
OrthoDBiEOG67430H.
PhylomeDBiP25894.

Family and domain databases

InterProiIPR001915. Peptidase_M48.
[Graphical view]
PfamiPF01435. Peptidase_M48. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIRALLVAM SVATVLTGCQ NMDSNGLLSS GAEAFQAYSL SDAQVKTLSD
60 70 80 90 100
QACQEMDSKA TIAPANSEYA KRLTTIANAL GNNINGQPVN YKVYMAKDVN
110 120 130 140 150
AFAMANGCIR VYSGLMDMMT DNEVEAVIGH EMGHVALGHV KKGMQVALGT
160 170 180 190 200
NAVRVAAASA GGIVGSLSQS QLGNLGEKLV NSQFSQRQEA EADDYSYDLL
210 220 230 240 250
RQRGISPAGL ATSFEKLAKL EEGRQSSMFD DHPASAERAQ HIRDRMSADG

IK
Length:252
Mass (Da):26,842
Last modified:October 1, 1996 - v2
Checksum:iE4C4718073B5C5B6
GO

Sequence cautioni

The sequence AAA69103.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAA83911.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32363 Genomic DNA. Translation: AAA83911.1. Different initiation.
U28377 Genomic DNA. Translation: AAA69103.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75973.2.
AP009048 Genomic DNA. Translation: BAE76999.1.
PIRiG65078.
RefSeqiNP_417411.2. NC_000913.3.
WP_001326497.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75973; AAC75973; b2936.
BAE76999; BAE76999; BAE76999.
GeneIDi945173.
KEGGiecj:JW2903.
eco:b2936.
PATRICi32121284. VBIEscCol129921_3030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32363 Genomic DNA. Translation: AAA83911.1. Different initiation.
U28377 Genomic DNA. Translation: AAA69103.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75973.2.
AP009048 Genomic DNA. Translation: BAE76999.1.
PIRiG65078.
RefSeqiNP_417411.2. NC_000913.3.
WP_001326497.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP25894.
SMRiP25894. Positions 91-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263066. 14 interactions.
DIPiDIP-12186N.
IntActiP25894. 3 interactions.
MINTiMINT-1288575.
STRINGi511145.b2936.

Protein family/group databases

MEROPSiM48.A04.

Proteomic databases

EPDiP25894.
PaxDbiP25894.
PRIDEiP25894.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75973; AAC75973; b2936.
BAE76999; BAE76999; BAE76999.
GeneIDi945173.
KEGGiecj:JW2903.
eco:b2936.
PATRICi32121284. VBIEscCol129921_3030.

Organism-specific databases

EchoBASEiEB1268.
EcoGeneiEG11291. loiP.

Phylogenomic databases

eggNOGiENOG4108K0D. Bacteria.
COG0501. LUCA.
HOGENOMiHOG000264551.
InParanoidiP25894.
KOiK07387.
OMAiMFDSHPG.
OrthoDBiEOG67430H.
PhylomeDBiP25894.

Enzyme and pathway databases

BioCyciEcoCyc:EG11291-MONOMER.
ECOL316407:JW2903-MONOMER.
MetaCyc:EG11291-MONOMER.

Miscellaneous databases

PROiP25894.

Family and domain databases

InterProiIPR001915. Peptidase_M48.
[Graphical view]
PfamiPF01435. Peptidase_M48. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli."
    Szumanski M.B.W., Boyle S.M.
    J. Bacteriol. 172:538-547(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Influence of cyclic AMP, agmatine, and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli."
    Szumanski M.B.W., Boyle S.M.
    J. Bacteriol. 174:758-764(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Up-regulation of yggG promotes the survival of Escherichia coli cells containing Era-1 mutant protein."
    Huang Y., Zhang B., Dong K., Zhang X., Hou L., Wang T., Chen N., Chen S.
    FEMS Microbiol. Lett. 275:8-15(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ERA, INDUCTION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Expression and regulation of the yggG gene of Escherichia coli."
    Huang Y., Dong K., Zhang X., Zhang B., Hou L., Chen N., Chen S.
    Curr. Microbiol. 56:14-20(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds."
    Lutticke C., Hauske P., Lewandrowski U., Sickmann A., Kaiser M., Ehrmann M.
    Mol. Biosyst. 8:1775-1782(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A PROTEASE, INTERACTION WITH BEPA, SUBCELLULAR LOCATION, INDUCTION, DISULFIDE BOND, GENE NAME.

Entry informationi

Entry nameiLOIP_ECOLI
AccessioniPrimary (citable) accession number: P25894
Secondary accession number(s): P76646, Q2M9Q7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 1, 1996
Last modified: March 16, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.