PRTV_VIBCM
ID PRTV_VIBCM Reviewed; 918 AA.
AC C3LUP3;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Pre-pro-metalloprotease PrtV {ECO:0000303|PubMed:23905008};
DE EC=3.4.24.- {ECO:0000305};
DE Contains:
DE RecName: Full=Pro-metalloprotease PrtV {ECO:0000250|UniProtKB:Q9KMU6};
DE Contains:
DE RecName: Full=37 kDa metalloprotease PrtV {ECO:0000250|UniProtKB:Q9KMU6};
DE Contains:
DE RecName: Full=18 kDa metalloprotease PrtV {ECO:0000250|UniProtKB:Q9KMU6};
DE Flags: Precursor;
GN Name=prtV {ECO:0000312|EMBL:ACP07198.1};
GN OrderedLocusNames=VCM66_A0219 {ECO:0000312|EMBL:ACP07198.1};
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2 {ECO:0000312|EMBL:ACP07198.1,
RC ECO:0000312|Proteomes:UP000001217};
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 755-839 IN COMPLEX WITH CALCIUM
RP ION.
RX PubMed=23905008; DOI=10.1016/j.fob.2013.06.003;
RA Edwin A., Rompikuntal P., Bjorn E., Stier G., Wai S.N.,
RA Sauer-Eriksson A.E.;
RT "Calcium binding by the PKD1 domain regulates interdomain flexibility in
RT Vibrio cholerae metalloprotease PrtV.";
RL FEBS Open Bio 3:263-270(2013).
CC -!- FUNCTION: Metalloprotease that exhibits a cytotoxic effect leading to
CC cell death. In host tissues, it could play a role in pathogenesis by
CC modulating the stability of the extracellular matrix components such as
CC fibronectin and fibrinogen. Also able to cleave plasminogen.
CC {ECO:0000250|UniProtKB:Q9KMU6}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9KMU6};
CC -!- ACTIVITY REGULATION: Calcium plays an important structural role,
CC providing stability to this protein in the cytoplasm. Outside the cell,
CC the decrease of the calcium concentration triggers the autoproteolysis.
CC {ECO:0000250|UniProtKB:Q9KMU6}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9KMU6}.
CC -!- PTM: PrtV is expressed as an inactive, multidomain, 102 kDa pre-pro-
CC metalloprotease. To form a catalytically active protease, PrtV is first
CC secreted, and then it undergoes N- and C-terminal cleavages during
CC envelope translocation to yield a 81 kDa pro-metalloprotease. Outside
CC the cell, the 81 kDa pro-metalloprotease undergoes an auto-cleavage.
CC The two major products of autoproteolysis (37 kDa and 18 kDa) together
CC form the so called 55 kDa active complex.
CC {ECO:0000250|UniProtKB:Q9KMU6}.
CC -!- SIMILARITY: Belongs to the peptidase M6 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001234; ACP07198.1; -; Genomic_DNA.
DR RefSeq; WP_000848953.1; NC_012580.1.
DR PDB; 4L9D; X-ray; 1.10 A; A/B=755-839.
DR PDBsum; 4L9D; -.
DR AlphaFoldDB; C3LUP3; -.
DR SMR; C3LUP3; -.
DR MEROPS; M06.002; -.
DR EnsemblBacteria; ACP07198; ACP07198; VCM66_A0219.
DR KEGG; vcm:VCM66_A0219; -.
DR HOGENOM; CLU_010858_1_0_6; -.
DR OMA; WAHRWYA; -.
DR Proteomes; UP000001217; Chromosome II.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR012300; Pept_M6_InhA.
DR InterPro; IPR008757; Peptidase_M6-like_domain.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR Pfam; PF05547; Peptidase_M6; 1.
DR Pfam; PF00801; PKD; 1.
DR PIRSF; PIRSF007519; Protease_InhA; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF49299; SSF49299; 2.
DR TIGRFAMs; TIGR03296; M6dom_TIGR03296; 1.
DR PROSITE; PS50093; PKD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Calcium; Cytolysis; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Repeat; Secreted; Signal;
KW Virulence; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..105
FT /evidence="ECO:0000250|UniProtKB:Q9KMU6"
FT /id="PRO_0000440249"
FT CHAIN 106..834
FT /note="Pro-metalloprotease PrtV"
FT /id="PRO_5002927614"
FT CHAIN 106..434
FT /note="37 kDa metalloprotease PrtV"
FT /evidence="ECO:0000250|UniProtKB:Q9KMU6"
FT /id="PRO_0000440250"
FT CHAIN 587..749
FT /note="18 kDa metalloprotease PrtV"
FT /evidence="ECO:0000250|UniProtKB:Q9KMU6"
FT /id="PRO_0000440251"
FT PROPEP 835..918
FT /evidence="ECO:0000250|UniProtKB:Q9KMU6"
FT /id="PRO_0000440252"
FT DOMAIN 758..835
FT /note="PKD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 855..918
FT /note="PKD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 757
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23905008"
FT BINDING 782
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23905008"
FT BINDING 821
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23905008"
FT BINDING 825
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23905008"
FT STRAND 763..768
FT /evidence="ECO:0007829|PDB:4L9D"
FT STRAND 771..776
FT /evidence="ECO:0007829|PDB:4L9D"
FT STRAND 781..783
FT /evidence="ECO:0007829|PDB:4L9D"
FT STRAND 785..791
FT /evidence="ECO:0007829|PDB:4L9D"
FT STRAND 793..795
FT /evidence="ECO:0007829|PDB:4L9D"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:4L9D"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:4L9D"
FT STRAND 811..821
FT /evidence="ECO:0007829|PDB:4L9D"
FT STRAND 826..835
FT /evidence="ECO:0007829|PDB:4L9D"
SQ SEQUENCE 918 AA; 101882 MW; 4F874BAFBD63FD07 CRC64;
MKTIKKTLLA AAIASFFSSG LYAQTPIDLG VVNEDKLIEM LVRTGQIPAD ASDVDKRIAL
ERYLEEKIRS GFKGDAQFGK KALEQRAKIL KVIDKQKGPH KARVFALDVG QKRTDKVLAL
LIDFPDLPWD DNRLTKEHTE MLYDRYEPSH YQDLLFSDKG YTGPNGENFI SMRQYYESES
GNSYSVSGQA AGWYRASKNA AYYGGNSPGT NNDMNARELV REALDQLARD PNINLADYDI
EDRYDYNGNG NFREPDGVID HLMIFHASVG EEAGGGVLGA DAIWSHRFNL GRYHVLEGTK
SNVPGRFNGQ FAAFDYTIQP IDAAAGVCAH EYGHDLGLPD EYDTQYTGTG EPVSYWSIMS
SGSWAGKIGG TQPTAFSSWA KQFLQNSIGG RWINHEQLSI NELEAKPRVV TLFQTTDNSR
PNMVKVTLPM KRVEGIKPAE GEFSFYSNRG DDLKNRMSRP LTIPAGSQAT LRFKAWFQIE
KDYDYARVLI NGKPIAGNIT TMDDPFKSGL VPAISGQSDG WVDAQFDLSA WAGQTVELAF
DYLTDGGLAM EGLYVDDLRL EVDGNQTLID NAEGTSSFAF QGFTKNGGFH EANHYYLLQW
RSHNDVDQGL ANLKRFGQLM SFEPGLLVWY VDESYADNWV GKHPGEGWLG VVDADQNALV
WSKTGEVAQT RFQVRDATFS LFDQAPLKLV TADGNTLEDM NLTANASFSD DQDYSSPQAP
DSGRKVMPFG LKIDLLSQSK ENEYGVVRLS KVTTENIAPV ARFELKVEGL SVMSQNTSSD
SDGNIVSYLW DFGNGQTSTE AAPTWSYTKA GSYSVTLTVT DDKGDSDTHQ QTIKVDTPNA
LPQASANYIH LGRWVTMWST STDSDGRIVD TEWTLPNGKI KRGRMFTAIF PSYGHHDVQL
KVMDDRGAVT TITIKVKL
