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Protein

Neutral protease

Gene

nprV

Organism
Vibrio proteolyticus (Aeromonas proteolytica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Extracellular zinc metalloprotease.

Catalytic activityi

Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favored residue, which distinguished this enzyme from thermolysin.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi343 – 3431Zinc; catalyticPROSITE-ProRule annotation
Active sitei344 – 3441PROSITE-ProRule annotation
Metal bindingi347 – 3471Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi367 – 3671Zinc; catalyticPROSITE-ProRule annotation
Active sitei426 – 4261Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.25. 167.

Protein family/group databases

MEROPSiM04.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral protease (EC:3.4.24.25)
Alternative name(s):
Aeromonolysin
Vibriolysin
Gene namesi
Name:nprV
OrganismiVibrio proteolyticus (Aeromonas proteolytica)
Taxonomic identifieri671 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Propeptidei25 – 196172Sequence analysisPRO_0000028630Add
BLAST
Chaini197 – 609413Neutral proteasePRO_0000028631Add
BLAST

Keywords - PTMi

Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ00971.
SMRiQ00971. Positions 199-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M4 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK08604.

Family and domain databases

Gene3Di3.10.170.10. 1 hit.
InterProiIPR011096. FTP_domain.
IPR025711. PepSY.
IPR007280. Peptidase_C_arc/bac.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]
PRINTSiPR00730. THERMOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q00971-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKTQRHINW LLAVSAATAL PVTAAEMINV NDGSLLNQAL KAQSQSVAPV
60 70 80 90 100
ETGFKQMKRV VLPNGKVKVR YQQTHHGLPV FNTSVVATES KSGSSEVFGV
110 120 130 140 150
MAQGIADDVS TLTPSVEMKQ AISIAKSRFQ QQEKMVAEPA TENEKAELMV
160 170 180 190 200
RLDDNNQAQL VYLVDFFVAE DHPARPFFFI DAQTGEVLQT WDGLNHAQAD
210 220 230 240 250
GTGPGGNTKT GRYEYGSDFP PFVIDKVGTK CSMNNSAVRT VDLNGSTSGN
260 270 280 290 300
TTYSYTCNDS TNYNDYKAIN GAYSPLNDAH YFGKVVFDMY KDWMNTTPLT
310 320 330 340 350
FQLTMRVHYG NNYENAFWNG SSMTFGDGYS TFYPLVDINV SAHEVSHGFT
360 370 380 390 400
EQNSGLVYEN MSGGMNEAFS DIAGEAAEFY MKGSVDWVVG ADIFKSSGGL
410 420 430 440 450
RYFDQPSRDG RSIDHASDYY NGLNVHYSSG VFNRAFYLLA NKAGWDVRKG
460 470 480 490 500
FEVFTLANQL YWTANSTFDE GGCGVVKAAS DMGYSVADVE DAFNTVGVNA
510 520 530 540 550
SCGATPPPSG DVLEIGKPLA NLSGNRNDMT YYTFTPSSSS SVVIKITGGT
560 570 580 590 600
GDADLYVKAG SKPTTTSYDC RPYKYGNEEQ CSISAQAGTT YHVMLRGYSN

YAGVTLRAD
Length:609
Mass (Da):66,363
Last modified:April 1, 1993 - v1
Checksum:i8FAB1798D737FC42
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64809 Genomic DNA. Translation: AAA27548.1.
PIRiJT0903.

Genome annotation databases

KEGGiag:AAA27548.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64809 Genomic DNA. Translation: AAA27548.1.
PIRiJT0903.

3D structure databases

ProteinModelPortaliQ00971.
SMRiQ00971. Positions 199-498.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM04.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA27548.

Phylogenomic databases

KOiK08604.

Enzyme and pathway databases

BRENDAi3.4.24.25. 167.

Family and domain databases

Gene3Di3.10.170.10. 1 hit.
InterProiIPR011096. FTP_domain.
IPR025711. PepSY.
IPR007280. Peptidase_C_arc/bac.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]
PRINTSiPR00730. THERMOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus."
    David V.A., Deutch A.H., Sloma A., Pawlyk D., Ally A., Durham D.R.
    Gene 112:107-112(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 197-215.

Entry informationi

Entry nameiNPRV_VIBPR
AccessioniPrimary (citable) accession number: Q00971
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: March 16, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.