PRTV_VIBCH
ID PRTV_VIBCH Reviewed; 918 AA.
AC Q9KMU6;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Pre-pro-metalloprotease PrtV {ECO:0000303|PubMed:18479458};
DE EC=3.4.24.- {ECO:0000305};
DE Contains:
DE RecName: Full=Pro-metalloprotease PrtV {ECO:0000303|PubMed:18479458};
DE Contains:
DE RecName: Full=37 kDa metalloprotease PrtV {ECO:0000303|PubMed:18479458};
DE Contains:
DE RecName: Full=18 kDa metalloprotease PrtV {ECO:0000303|PubMed:18479458};
DE Flags: Precursor;
GN Name=prtV {ECO:0000303|PubMed:9371455};
GN OrderedLocusNames=VC_A0223 {ECO:0000312|EMBL:AAF96135.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, AND NOMENCLATURE.
RX PubMed=9371455; DOI=10.1128/jb.179.22.7072-7080.1997;
RA Ogierman M.A., Fallarino A., Riess T., Williams S.G., Attridge S.R.,
RA Manning P.A.;
RT "Characterization of the Vibrio cholerae El Tor lipase operon lipAB and a
RT protease gene downstream of the hly region.";
RL J. Bacteriol. 179:7072-7080(1997).
RN [3]
RP PROTEIN SEQUENCE OF 106-434, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND PROTEIN PROCESSING.
RX PubMed=18479458; DOI=10.1111/j.1742-4658.2008.06470.x;
RA Vaitkevicius K., Rompikuntal P.K., Lindmark B., Vaitkevicius R., Song T.,
RA Wai S.N.;
RT "The metalloprotease PrtV from Vibrio cholerae.";
RL FEBS J. 275:3167-3177(2008).
RN [4]
RP FUNCTION, COFACTOR, AND PROTEIN PROCESSING.
RX PubMed=24492010; DOI=10.1016/j.pep.2014.01.012;
RA Edwin A., Grundstroem C., Wai S.N., Ohman A., Stier G.,
RA Sauer-Eriksson A.E.;
RT "Domain isolation, expression, purification and proteolytic activity of the
RT metalloprotease PrtV from Vibrio cholerae.";
RL Protein Expr. Purif. 96:39-47(2014).
RN [5]
RP STRUCTURE BY NMR OF 23-103.
RX PubMed=26434928; DOI=10.1002/pro.2815;
RA Edwin A., Persson C., Mayzel M., Wai S.N., Ohman A., Karlsson B.G.,
RA Sauer-Eriksson A.E.;
RT "Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio
RT cholerae.";
RL Protein Sci. 24:2076-2080(2015).
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:0000269|PubMed:18479458, ECO:0000269|PubMed:24492010,
CC ECO:0000305|PubMed:9371455}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:24492010};
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 PrtV activity is increased by 25 mM of Sr(2+) or Mg(2+) and to some
CC extent by Ba(2+); however, Ba(2+) inhibits PrtV at higher
CC concentrations. Completely inhibited by EDTA and 1,10-phenanthroline.
CC {ECO:0000269|PubMed:18479458}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18479458}.
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. {ECO:0000269|PubMed:18479458,
CC ECO:0000269|PubMed:24492010}.
CC -!- SIMILARITY: Belongs to the peptidase M6 family. {ECO:0000305}.
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DR EMBL; AE003853; AAF96135.1; -; Genomic_DNA.
DR PIR; E82486; E82486.
DR RefSeq; NP_232622.1; NC_002506.1.
DR RefSeq; WP_000848953.1; NZ_LT906615.1.
DR PDB; 5ABK; NMR; -; A=23-103.
DR PDBsum; 5ABK; -.
DR AlphaFoldDB; Q9KMU6; -.
DR BMRB; Q9KMU6; -.
DR SMR; Q9KMU6; -.
DR STRING; 243277.VC_A0223; -.
DR MEROPS; M06.002; -.
DR PRIDE; Q9KMU6; -.
DR EnsemblBacteria; AAF96135; AAF96135; VC_A0223.
DR KEGG; vch:VC_A0223; -.
DR PATRIC; fig|243277.26.peg.2856; -.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG4412; Bacteria.
DR HOGENOM; CLU_010858_1_0_6; -.
DR OMA; WAHRWYA; -.
DR BioCyc; VCHO:VCA0223-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
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;
KW Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Repeat; Secreted; Signal; Virulence; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000305|PubMed:18479458"
FT PROPEP 24..105
FT /evidence="ECO:0000305|PubMed:18479458"
FT /id="PRO_0000440245"
FT CHAIN 106..834
FT /note="Pro-metalloprotease PrtV"
FT /id="PRO_5004328302"
FT CHAIN 106..434
FT /note="37 kDa metalloprotease PrtV"
FT /evidence="ECO:0000269|PubMed:18479458"
FT /id="PRO_0000440246"
FT CHAIN 587..749
FT /note="18 kDa metalloprotease PrtV"
FT /evidence="ECO:0000305|PubMed:18479458"
FT /id="PRO_0000440247"
FT PROPEP 835..918
FT /evidence="ECO:0000305|PubMed:18479458"
FT /id="PRO_0000440248"
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:0000250|UniProtKB:C3LUP3"
FT BINDING 782
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C3LUP3"
FT BINDING 821
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C3LUP3"
FT BINDING 825
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C3LUP3"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:5ABK"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:5ABK"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5ABK"
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
