FLS_FERPE
ID FLS_FERPE Reviewed; 699 AA.
AC Q93LQ6;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Fervidolysin {ECO:0000303|PubMed:12072953};
DE EC=3.4.21.- {ECO:0000269|PubMed:16535379};
DE AltName: Full=Keratinase {ECO:0000303|PubMed:16535379};
DE AltName: Full=Subtilisin-like serine protease {ECO:0000303|PubMed:12072953};
DE Flags: Precursor;
GN Name=fls {ECO:0000303|PubMed:12072953, ECO:0000312|EMBL:AAK61552.1};
OS Fervidobacterium pennivorans.
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=93466 {ECO:0000312|EMBL:AAK61552.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-37 AND 150-161,
RP MUTAGENESIS OF HIS-228, AUTO-PROTEOLYTIC PROCESSING, AND ACTIVE SITE.
RX PubMed=12072953; DOI=10.1007/s007920100239;
RA Kluskens L.D., Voorhorst W.G., Siezen R.J., Schwerdtfeger R.M.,
RA Antranikian G., van der Oost J., de Vos W.M.;
RT "Molecular characterization of fervidolysin, a subtilisin-like serine
RT protease from the thermophilic bacterium Fervidobacterium pennivorans.";
RL Extremophiles 6:185-194(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RX PubMed=16535379; DOI=10.1128/aem.62.8.2875-2882.1996;
RA Friedrich A.B., Antranikian G.;
RT "Keratin degradation by Fervidobacterium pennavorans, a novel thermophilic
RT anaerobic species of the order Thermotogales.";
RL Appl. Environ. Microbiol. 62:2875-2882(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 29-699 IN COMPLEX WITH CALCIUM,
RP AND DOMAIN.
RX PubMed=14687574; DOI=10.1016/j.jmb.2003.11.006;
RA Kim J.S., Kluskens L.D., de Vos W.M., Huber R., van der Oost J.;
RT "Crystal structure of fervidolysin from Fervidobacterium pennivorans, a
RT keratinolytic enzyme related to subtilisin.";
RL J. Mol. Biol. 335:787-797(2004).
CC -!- FUNCTION: Protease able to degrade keratin into peptides. Is
CC responsible for keratinolysis by F.pennivorans, which allows this
CC bacterium to grow on native feathers. {ECO:0000269|PubMed:16535379}.
CC -!- ACTIVITY REGULATION: Is inhibited by phenylmethylsulfonyl fluoride and
CC 3,4-dichloroisocoumarin. EDTA and iodoacetate (1 to 5 mM) have only
CC little effect on the enzyme activity. {ECO:0000269|PubMed:16535379}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 10. Is active in a broad pH range, namely, between pH
CC 6.0 and 10.5. {ECO:0000269|PubMed:16535379};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius. Is active in a broad
CC temperature range, namely, between 50 and 100 degrees Celsius.
CC Thermostable. {ECO:0000269|PubMed:16535379};
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16535379}.
CC Note=Is cell-bound, probably associated with the outer cell envelope.
CC {ECO:0000269|PubMed:16535379}.
CC -!- DOMAIN: Is composed of four domains: a catalytic domain, two beta-
CC sandwich domains that may mediate interactions with substrate, and the
CC propeptide domain. {ECO:0000269|PubMed:14687574}.
CC -!- PTM: Undergoes auto-proteolytic processing. Once cleaved, the
CC propeptide can remain associated with the protease and blocks its
CC activity. The physiological activation of fervidolysin is proposed to
CC be achieved through the stepwise removal of the propeptide accomplished
CC by several proteolytic cleavages that may not be autolytic.
CC {ECO:0000269|PubMed:12072953, ECO:0000269|PubMed:14687574}.
CC -!- BIOTECHNOLOGY: The thermostable keratinase of F.pennavorans is a
CC promising enzyme for application in an industrial process. Native
CC feathers produced as waste by poultry farming could be converted to
CC peptides and rare amino acids like proline and serine.
CC {ECO:0000305|PubMed:16535379}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AY035311; AAK61552.1; -; Genomic_DNA.
DR RefSeq; WP_014451857.1; NZ_CP050868.1.
DR PDB; 1R6V; X-ray; 1.70 A; A=29-699.
DR PDBsum; 1R6V; -.
DR AlphaFoldDB; Q93LQ6; -.
DR SMR; Q93LQ6; -.
DR MEROPS; S08.021; -.
DR OMA; WQIRKLL; -.
DR EvolutionaryTrace; Q93LQ6; -.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd07485; Peptidases_S8_Fervidolysin_like; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034063; Fervidolysin_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Calcium; Direct protein sequencing;
KW Hydrolase; Metal-binding; Protease; Serine protease; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000305|PubMed:12072953"
FT PROPEP 22..149
FT /evidence="ECO:0000305|PubMed:12072953"
FT /id="PRO_0000437885"
FT CHAIN 150..699
FT /note="Fervidolysin"
FT /id="PRO_5004320072"
FT DOMAIN 163..465
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000305|PubMed:12072953"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000305|PubMed:12072953"
FT ACT_SITE 409
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000305|PubMed:12072953"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:14687574,
FT ECO:0007744|PDB:1R6V"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:14687574,
FT ECO:0007744|PDB:1R6V"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:14687574,
FT ECO:0007744|PDB:1R6V"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:14687574,
FT ECO:0007744|PDB:1R6V"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:14687574,
FT ECO:0007744|PDB:1R6V"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:14687574,
FT ECO:0007744|PDB:1R6V"
FT MUTAGEN 228
FT /note="H->A: Blocks the proteolytic cleavage leading to
FT mature fervidolysin."
FT /evidence="ECO:0000269|PubMed:12072953"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1R6V"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1R6V"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1R6V"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 408..425
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 431..441
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:1R6V"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 461..466
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 471..483
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 524..533
FT /evidence="ECO:0007829|PDB:1R6V"
FT TURN 542..544
FT /evidence="ECO:0007829|PDB:1R6V"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 563..572
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 586..590
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 612..617
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 630..638
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 647..655
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 658..666
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 671..676
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 686..688
FT /evidence="ECO:0007829|PDB:1R6V"
FT STRAND 694..697
FT /evidence="ECO:0007829|PDB:1R6V"
SQ SEQUENCE 699 AA; 75057 MW; A3843EDDC3F1A4DA CRC64;
MRKVLLIASI VALILALFSC ANPSFEPRSK AKDLASLPEI KSQGYHILFG ELRDGEYTEG
KILVGYNDRS EVDKIVKAVN GKVVLELPQI KVVSIKLNGM TVKQAYDKIK ALALKGIRYV
EPSYKRELIK PTVVKPNPDM YKIRKPGLNS TARDYGEELS NELWGLEAIG VTQQLWEEAS
GTNIIVAVVD TGVDGTHPDL EGQVIAGYRP AFDEELPAGT DSSYGGSHGT HVAGTIAAKK
DGKGIVGVAP GAKIMPIVIF DDPALVGGNG YVGDDYVAAG IIWATDHGAK VMNHSWGGWG
YSYTMKEAFD YAMEHGVVMV VSAGNNTSDS HHQYPAGYPG VIQVAALDYY GGTFRVAGFS
SRSDGVSVGA PGVTILSTVP GEDSIGYEGH NENVPATNGG TYDYYQGTSM AAPHVTGVVA
VLLQKFPNAK PWQIRKLLEN TAFDFNGNGW DHDTGYGLVK LDAALQGPLP TQGGVEEFQV
VVTDAKGNFG VPTVFVSMMR DNGSCYYAKT GPDGIARFPH IDSGTYDIFV GGPDHWDRAL
APYDGESIPG GYAIALRMAE ERQASFVGFG VSPDATQLNV NFNSTLQVKF STNLSTLKDP
QFVVVDPLLR GVYGRVAYAR NQTYDLSLLS GQISFGIQTL LPAATDITIQ GTVTLNGEDI
PVYGVLKAGT TWTIIDDFGG LNLGTDSQPI YVWWTIFGQ
