SASDFB6: The periplasmically localised protease PqqL from Escherichia coli

Basic information

• Entry: Database: SASBDB / ID: SASDFB6

Sample

The periplasmically localised protease PqqL from Escherichia coli

• Zinc protease PqqL (protein), Escherichia coli (strain K12)

Function / homology

Function:

Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / metalloendopeptidase activity / metallopeptidase activity / outer membrane-bounded periplasmic space / peptidase activity / proteolysis / zinc ion binding / cytosol

Domain/homology:

Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like

Component:

Probable zinc protease PqqL

• Biological species: Escherichia coli (strain K12) (bacteria)
• Citation: Journal: PLoS Genet / Year: 2019; Title: Protease-associated import systems are widespread in Gram-negative bacteria.; Authors: Rhys Grinter / Pok Man Leung / Lakshmi C Wijeyewickrema / Dene Littler / Simone Beckham / Robert N Pike / Daniel Walker / Chris Greening / Trevor Lithgow / ; Abstract: Bacteria have evolved sophisticated uptake machineries in order to obtain the nutrients required for growth. Gram-negative plant pathogens of the genus Pectobacterium obtain iron from the protein ferredoxin, which is produced by their plant hosts. This iron-piracy is mediated by the ferredoxin uptake system (Fus), a gene cluster encoding proteins that transport ferredoxin into the bacterial cell and process it proteolytically. In this work we show that gene clusters related to the Fus are widespread in bacterial species. Through structural and biochemical characterisation of the distantly related Fus homologues YddB and PqqL from Escherichia coli, we show that these proteins are analogous to components of the Fus from Pectobacterium. The membrane protein YddB shares common structural features with the outer membrane ferredoxin transporter FusA, including a large extracellular substrate binding site. PqqL is an active protease with an analogous periplasmic localisation and iron-dependent expression to the ferredoxin processing protease FusC. Structural analysis demonstrates that PqqL and FusC share specific features that distinguish them from other members of the M16 protease family. Taken together, these data provide evidence that protease associated import systems analogous to the Fus are widespread in Gram-negative bacteria.

Contact author

• Grinter Grinter (Monash University, Melbourne, Australia)

Models

• Model #2983: ; Type: dummy / Radius of dummy atoms: 3.50 A / Chi-square value: 0.506 / P-value: 0.003869; Search similar-shape structures of this assembly by Omokage search (details)
• Model #2985: ; Type: dummy / Software: (5) / Radius of dummy atoms: 3.50 A / Symmetry: P1 / Chi-square value: 0.506 / P-value: 0.003869; Search similar-shape structures of this assembly by Omokage search (details)
• Model #2984: ; Type: atomic / Symmetry: P1 / Chi-square value: 9.541; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: The periplasmically localised protease PqqL from Escherichia coli; Specimen concentration: 8 mg/ml
• Buffer: Name: 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol / pH: 7.8

Entity #1638

Type: protein / Description: Zinc protease PqqL / Formula weight: 101.744 / Num. of mol.: 1 / Source: Escherichia coli (strain K12) / References: UniProt: P31828
Sequence:

AALPQDEKLI TGQLDNGLRY MIYPHAHPKD QVNLWLQIHT GSLQEEDNEL GVAHFVEHMM FNGTKTWPGN KVIETFESMG LRFGRDVNAY TSYDETVYQV SLPTTQKQNL QQVMAIFSEW SNAATFEKLE VDAERGVITE EWRAHQDAKW RTSQARRPFL LANTRNLDRE PIGLMDTVAT VTPAQLRQFY QRWYQPNNMT FIVVGDIDSK EALALIKDNL SKLPANKAAE NRVWPTKAEN HLRFNIINDK ENRVNGIALY YRLPMVQVND EQSFIEQAEW SMLVQLFNQR LQERIQSGEL KTISGGTARS VKIAPDYQSL FFRVNARDDN MQDAANALMA ELATIDQHGF SAEELDDVKS TRLTWLKNAV DQQAERDLRM LTSRLASSSL NNTPFLSPEE TYQLSKRLWQ QITVQSLAEK WQQLRKNQDA FWEQMVNNEV AAKKALSPAA ILALEKEYAN KKLAAYVFPG RNLSLTVDAD PQAEISSKET LAENLTSLTL SNGARVILAK SAGEEQKLQI IAVSNKGDLS FPAQQKSLIA LANKAVSGSG VGELSSSSLK RWSAENSVTM SSKVSGMNTL LSVSARTNNP EPGFQLINQR ITHSTINDNI WASLQNAQIQ ALKTLDQRPA EKFAQQMYET RYADDRTKLL QENQIAQFTA ADALAADRQL FSSPADITFV IVGNVAEDKL VALITRYLGS IKHSDSPLAA GKPLTRATDN ASVTVKEQNE PVAQVSQWKR YDSRTPVNLP TRMALDAFNV ALAKDLRVNI REQASGAYSV SSRLSVDPQA KDISHLLAFT CQPERHDELL TLANEVMVKR LAKGISEQEL NEYQQNVQRS LDIQQRSVQQ LANTIVNSLI QYDDPAAWTE QEQLLKQMTV ENVNTAVKQY LSHPVNTYTG VLLPK

Experimental information

• Beam: Instrument name: Australian Synchrotron SAXS/WAXS / City: Melbourne / 国: Australia / Shape: Point / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.10322 Å / Dist. spec. to detc.: 1.426 mm
• Detector: Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm

Scan

Title: The periplasmically localised protease PqqL from Escherichia coli
Measurement date: Jun 14, 2017 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/A /

	Min	Max
Q	0.0057	0.3188

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 523 /

	Min	Max
Q	0.00786314	0.198693
P(R) point	1	523
R	0	136.9

Result

Type of curve: sec /

	Experimental	Porod
MW	113 kDa	130 kDa
Volume	-	207 nm3

	P(R)	Guinier	Guinier error
Forward scattering, I0	0.08263	0.13678	0.0002
Radius of gyration, Rg	4.11 nm	4.02 nm	0.88

	Min	Max
D	-	13.69
Guinier point	7	70