GELE_ENTFA
ID GELE_ENTFA Reviewed; 510 AA.
AC Q833V7; A1E464; B5AN27; Q47786; Q9S385;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Gelatinase {ECO:0000303|PubMed:1846126, ECO:0000312|EMBL:ACF74544.2};
DE EC=3.4.24.30;
DE AltName: Full=Coccolysin {ECO:0000303|PubMed:8179636, ECO:0000312|EMBL:AAO81586.1};
DE Flags: Precursor;
GN Name=gelE {ECO:0000303|PubMed:1846126, ECO:0000312|EMBL:ABL10087.1};
GN OrderedLocusNames=EF_1818;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA24778.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 193-200.
RC STRAIN=OG1-10 {ECO:0000269|PubMed:1846126};
RX PubMed=1846126; DOI=10.1128/iai.59.1.415-420.1991;
RA Su Y.A., Sulavik M.C., He P., Makinen K.K., Makinen P.L., Fiedler S.,
RA Wirth R., Clewell D.B.;
RT "Nucleotide sequence of the gelatinase gene (gelE) from Enterococcus
RT faecalis subsp. liquefaciens.";
RL Infect. Immun. 59:415-420(1991).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA12802.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23655 / NBRC 3989 / NCDO 592;
RX PubMed=16232519; DOI=10.1016/s1389-1723(99)80115-7;
RA Kirimura K., Kamigaki K., Ebihara T., Ishii Y., Kanayama S., Usami S.;
RT "Determination of nucleotide sequence related to the plasmid replication
RT region in Enterococcus faecalis and its application to a new shuttle
RT vector.";
RL J. Biosci. Bioeng. 87:566-571(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:ABL10087.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=GM {ECO:0000269|PubMed:17261598};
RX PubMed=17261598; DOI=10.1128/iai.01473-06;
RA Park S.Y., Kim K.M., Lee J.H., Seo S.J., Lee I.H.;
RT "Extracellular gelatinase of Enterococcus faecalis destroys a defense
RT system in insect hemolymph and human serum.";
RL Infect. Immun. 75:1861-1869(2007).
RN [4] {ECO:0000312|EMBL:AAO81586.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [5] {ECO:0000305, ECO:0000312|EMBL:ACF74544.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-502.
RC STRAIN=H81 {ECO:0000312|EMBL:ACF74544.2};
RX PubMed=19222538; DOI=10.1111/j.1462-2920.2009.01881.x;
RA Macovei L., Ghosh A., Thomas V.C., Hancock L.E., Mahmood S., Zurek L.;
RT "Enterococcus faecalis with the gelatinase phenotype regulated by the fsr
RT operon and with biofilm-forming capacity are common in the agricultural
RT environment.";
RL Environ. Microbiol. 11:1540-1547(2009).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=2536744; DOI=10.1016/s0021-9258(18)94069-x;
RA Makinen P.L., Clewell D.B., An F., Makinen K.K.;
RT "Purification and substrate specificity of a strongly hydrophobic
RT extracellular metalloendopeptidase ('gelatinase') from Streptococcus
RT faecalis (strain 0G1-10).";
RL J. Biol. Chem. 264:3325-3334(1989).
RN [7] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8179636; DOI=10.1006/bbrc.1994.1546;
RA Makinen P.L., Makinen K.K.;
RT "The Enterococcus faecalis extracellular metalloendopeptidase (EC
RT 3.4.24.30; coccolysin) inactivates human endothelin at bonds involving
RT hydrophobic amino acid residues.";
RL Biochem. Biophys. Res. Commun. 200:981-985(1994).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=12775699; DOI=10.1128/jb.185.12.3613-3623.2003;
RA Waters C.M., Antiporta M.H., Murray B.E., Dunny G.M.;
RT "Role of the Enterococcus faecalis GelE protease in determination of
RT cellular chain length, supernatant pheromone levels, and degradation of
RT fibrin and misfolded surface proteins.";
RL J. Bacteriol. 185:3613-3623(2003).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=18941224; DOI=10.4049/jimmunol.181.9.6328;
RA Park S.Y., Shin Y.P., Kim C.H., Park H.J., Seong Y.S., Kim B.S., Seo S.J.,
RA Lee I.H.;
RT "Immune evasion of Enterococcus faecalis by an extracellular gelatinase
RT that cleaves C3 and iC3b.";
RL J. Immunol. 181:6328-6336(2008).
CC -!- FUNCTION: Metalloprotease capable of the hydrolysis of insoluble
CC hydrophobic substrates. Hydrolyzes azocoll and gelatin and, at a lower
CC rate, soluble and insoluble collagens. Does not cleave short synthetic
CC peptides. Preferentially hydrolyzes the 24-Phe-|-Phe-25 bond in the
CC insulin B-chain, followed by the 5-His-|-Leu-6 bond. Inactivates
CC endothelin-1, primarily by cleavage of the 5-Ser-|-Leu-6 and 16-His-|-
CC Leu-17 bonds. Hydrolyzes the alpha chain of C3 to generate a C3b-like
CC protein. Inhibits complement-mediated hemolysis and opsinization of
CC bacteria. Hydrolyzes the insect antimicrobial peptide cecropin.
CC Decreases the length of E.faecalis chains via the activation of
CC autolysin. Degrades polymerized fibrin. {ECO:0000269|PubMed:12775699,
CC ECO:0000269|PubMed:17261598, ECO:0000269|PubMed:18941224,
CC ECO:0000269|PubMed:2536744, ECO:0000269|PubMed:8179636}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Xaa-|-Leu, Xaa-|-Phe, Xaa-|-Tyr, Xaa-|-
CC Ala.; EC=3.4.24.30; Evidence={ECO:0000269|PubMed:2536744,
CC ECO:0000269|PubMed:8179636};
CC -!- ACTIVITY REGULATION: Inhibited by L-leucine hydroxamate and
CC phosphoramidon. Not inhibited by phenylmethanesulfonyl fluoride.
CC Reversibly inactivated by straight-chain aliphatic alcohols.
CC {ECO:0000269|PubMed:2536744}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.2. Active from pH 6.0-8.0, activity decreases rapidly
CC at more acidic pH values. Stable only above pH 5.6.
CC {ECO:0000269|PubMed:2536744};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17261598}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24778.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABL10087.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA12802.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M37185; AAA24778.1; ALT_INIT; Genomic_DNA.
DR EMBL; D85393; BAA12802.1; ALT_INIT; Genomic_DNA.
DR EMBL; EF105504; ABL10087.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE016830; AAO81586.1; -; Genomic_DNA.
DR EMBL; EU862241; ACF74544.2; -; Genomic_DNA.
DR PIR; A43580; A43580.
DR RefSeq; NP_815516.1; NC_004668.1.
DR RefSeq; WP_002369251.1; NZ_KE136528.1.
DR AlphaFoldDB; Q833V7; -.
DR SMR; Q833V7; -.
DR IntAct; Q833V7; 1.
DR STRING; 226185.EF_1818; -.
DR MEROPS; M04.007; -.
DR DNASU; 1200704; -.
DR EnsemblBacteria; AAO81586; AAO81586; EF_1818.
DR KEGG; efa:EF1818; -.
DR PATRIC; fig|226185.9.peg.1708; -.
DR eggNOG; COG3227; Bacteria.
DR HOGENOM; CLU_008590_5_2_9; -.
DR OMA; WKHIKLT; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..192
FT /evidence="ECO:0000255, ECO:0000269|PubMed:1846126"
FT /id="PRO_0000395367"
FT CHAIN 193..510
FT /note="Gelatinase"
FT /evidence="ECO:0000269|PubMed:1846126"
FT /id="PRO_0000395368"
FT ACT_SITE 329
FT /evidence="ECO:0000250|UniProtKB:P81177,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 419
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P81177,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81177"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P81177,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P81177,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P81177,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P81177"
FT CONFLICT 2
FT /note="Missing (in Ref. 5; ACF74544)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="R -> K (in Ref. 1; AAA24778, 2; BAA12802, 3;
FT ABL10087 and 5; ACF74544)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="I -> V (in Ref. 1; AAA24778)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="T -> N (in Ref. 2; BAA12802)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="V -> F (in Ref. 3; ABL10087)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..166
FT /note="PT -> LI (in Ref. 3; ABL10087)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="A -> T (in Ref. 1; AAA24778, 2; BAA12802 and 3;
FT ABL10087)"
FT /evidence="ECO:0000305"
FT CONFLICT 248..249
FT /note="VA -> AT (in Ref. 1; AAA24778, 2; BAA12802 and 3;
FT ABL10087)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="V -> A (in Ref. 5; ACF74544)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="V -> I (in Ref. 1; AAA24778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 55504 MW; 9E2E378D38BAC1D1 CRC64;
MMKGNKILYI LGTGIFVGSS CLFSSLFVAA EEQVYSESEV STVLSKLEKE AISEAAAEQY
TVVDRKEDAW GMKHLKLEKQ TEGVTVDSDN VIIHLDRNGA VTSVTGNPVD QVVKIQSVDA
IGEEGVKKII ASDNPETKDL VFLAIDKRVN NEGQLFYKVR VTSSPTGDPV SLVYKVNATD
GTIMEKQDLT EHVGSEVTLK NSFQVAFNVP VEKSNTGIAL HGTDNTGVYH AVVDGKNNYS
IIQAPSLVAL NQNAVDAYTH GKFVKTYYED HFQRHSIDDR GMPILSVVDE QHPDAYDNAF
WDGKAMRYGE TSTPTGKTYA SSLDVVGHEM THGVTEHTAG LEYLGQSGAL NESYSDLMGY
IISGASNPEI GADTQSVDRK TGIRNLQTPS KHGQPETMAQ YDDRARYKGT PYYDQGGVHY
NSGIINRIGY TIIQNLGIEK AQTIFYSSLV NYLTPKAQFS DARDAMLAAA KVQYGDEAAS
VVSAAFNSAG IGAKEDIQVN QPSESVLVNE
