ID E7NPZ5_TREPH Unreviewed; 610 AA.
AC E7NPZ5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN Name=pepF {ECO:0000313|EMBL:EFW39386.1};
GN ORFNames=HMPREF9554_00121 {ECO:0000313|EMBL:EFW39386.1};
OS Treponema phagedenis F0421.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=754027 {ECO:0000313|EMBL:EFW39386.1, ECO:0000313|Proteomes:UP000004157};
RN [1] {ECO:0000313|EMBL:EFW39386.1, ECO:0000313|Proteomes:UP000004157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0421 {ECO:0000313|EMBL:EFW39386.1,
RC ECO:0000313|Proteomes:UP000004157};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC bioactive peptides. {ECO:0000256|RuleBase:RU368091}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU368091};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU368091};
CC -!- SIMILARITY: Belongs to the peptidase M3B family.
CC {ECO:0000256|RuleBase:RU368091}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFW39386.1}.
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DR EMBL; AEFH01000008; EFW39386.1; -; Genomic_DNA.
DR RefSeq; WP_002695016.1; NZ_GL637961.1.
DR AlphaFoldDB; E7NPZ5; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_12; -.
DR Proteomes; UP000004157; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09608; 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 Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 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 InterPro; IPR004438; Peptidase_M3B.
DR NCBIfam; TIGR00181; pepF; 1.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368091};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368091};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU368091};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 120..192
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 214..592
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 610 AA; 69335 MW; A643E94445325857 CRC64;
MKSTTPKRAD IAKENQWKLE LLFESEQAWQ SALQEAIKSG ERVLLYKDTF ENPAEVESAT
LLNCLQAFET FEKQSEKLGQ YAFLKKSEDE GNSENIARLS QYIMAMTEIS AKLSWFVPAL
MQIPEDKVRA WIDPSGAEGK AFANYKIFIE KTLYLKVHTL SDREEKMLTL LSESGGTAQR
SFSVLTNVDL QFGSITDRGE EKELTQSSFS QFLLSPDRAV REKAYKQFYA GFDAHKNTIA
SLYIGQVQQN TAMAKIRGYG SARENALYPD KVPVSVYDNL IKSVRDNLEP LHRFYALVQK
TLKVEELRHY DVYVPLVAEI RKHTEYTEAV DIITEALQPL GGEYVNTIRS GLLGGWVDRY
ENQGKRSGAF SSGGFESEPY ILMNYKPDVI RDVFTLAHEG GHSMHSWYSV RNNPFLCHDY
TIFEAEVAST FNEELLFRSM VKKASDPKER AYLLSIRASD ILATLYRQTM FAEFEMITHQ
LVESGTPLTL DRLRAEYKKL LTAYFGPAMH FEEVSDLECL RIPHFYRAFY VYKYATGISA
SLALAERVLS GGETERNDYF NFLKSGGSRY PIEALKVAGV DMASPEPVRA ACNHFGEIVT
ELEKALKTIL
//
