ID A7HLF3_FERNB Unreviewed; 578 AA.
AC A7HLF3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Peptidase M3A and M3B thimet/oligopeptidase F {ECO:0000313|EMBL:ABS60736.1};
GN OrderedLocusNames=Fnod_0884 {ECO:0000313|EMBL:ABS60736.1};
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS60736.1, ECO:0000313|Proteomes:UP000002415};
RN [1] {ECO:0000313|EMBL:ABS60736.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABS60736.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CP000771; ABS60736.1; -; Genomic_DNA.
DR RefSeq; WP_011994052.1; NC_009718.1.
DR AlphaFoldDB; A7HLF3; -.
DR STRING; 381764.Fnod_0884; -.
DR KEGG; fno:Fnod_0884; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_3_0_0; -.
DR OrthoDB; 9769691at2; -.
DR Proteomes; UP000002415; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09610; M3B_PepF; 1.
DR Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF08439; Peptidase_M3_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000002415};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 103..166
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 185..563
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT COILED 35..89
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 578 AA; 67575 MW; DA426B167B84F4BE CRC64;
MQWDFKTVFQ SDEEAIENAK RYSKLIGSLV DELEKEKELN KIIKLIKEIE DSTDNFSKSI
QYAWMRYSVN TKEKESQKLL GTIQSLESNV GEYFAKLEVR LSKLSKKDIQ ELKKIAPNYT
HFIEVIEKRK KHLLSKEAEQ VLALTSISRR EAISKIHNKL ESSYKFKIEI DGEIKVLTPE
EVKALRRSTN SDLRKKAMKT FLKRFQEDSL VITEVYNLVV KDYDLESKIR KFARPISMRN
FENEVSDDVV DSLIETTNEN VNILREYYKW KSEVMNEKLT LADIYAPITT KARKFSFDEA
KEIILDAYYS FSNKAGDIVK SFFENSRIDL YPREGKIGGA YCIYSTTKLP AYVLTNFNGD
MYDIMTLAHE LGHGLHGTLS KKQTYFNYDT PLTLAELASV FGEFLVFDYL KGKLDKEERL
ALISSKIEDT FATTFRQNFF TNFEIRSHDL ISNSGYADWE ELNDIYYEEL RKTFGEVVEI
PQWYKNEWAM ISHFFETPFY VYSYNFAHCL VIALYQKYLE EGKSFTKKYL SLLESGGSLS
PNELLSKVGI DISRSDFWEK AFDFIDSLVK EIKINYNK
//
