ID A0A239PX11_9RHOB Unreviewed; 607 AA.
AC A0A239PX11;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:SNT74476.1};
GN ORFNames=SAMN05444959_1086 {ECO:0000313|EMBL:SNT74476.1};
OS Paracoccus seriniphilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=184748 {ECO:0000313|EMBL:SNT74476.1, ECO:0000313|Proteomes:UP000198307};
RN [1] {ECO:0000313|EMBL:SNT74476.1, ECO:0000313|Proteomes:UP000198307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14827 {ECO:0000313|EMBL:SNT74476.1,
RC ECO:0000313|Proteomes:UP000198307};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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; FZQB01000008; SNT74476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239PX11; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000198307; Unassembled WGS sequence.
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 InterPro; IPR011977; Pept_M3B_clade3.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
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 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:UP000198307};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 126..195
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 348..590
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 607 AA; 67714 MW; 2FA3BB12B454E40A CRC64;
MAGHMNFDSV EQTKGTAFGD LPEWDLNDLY PGPDSPELKS DLESLSTQVE TFAKRYQGKL
ADLGPAEMLD CIREYEAIDI IAGQVMSYAG LRYYQNTTDA DRAKMLGDLQ ARITDITTAL
VFFSLEFNRI PDETYEAVFA ATDGPARYKP VFDRMRAMRP HQLSDELEQF LHDNSVVGAA
AWNRLFDETT ASLEFSVNGE TMGLEATLNL LTEHDRDQRE AAARALAKVF GDNIKLFSRI
HNTLAKEKAI EDKWRKMPSP QHGRHLSNHV EPEVVEALRN AVTQAYPRLS HRYYALKAKW
LGLDKLQIWD RNAPLPTDAP RTIGWDEARS TVLDAYAGFA PELAELAKPF FDKGWIDAAV
KPGKAPGAFA HPTVTTVHPY VLLNYLGKPR DVMTLAHELG HGVHQRLAAK QGELLASTPL
TLAETASVFG EMLTFRALLA KTTDPAQKKA LLAGKVEDMI NTVVRQIAFY DFECKLHAAR
AEGELTPDDI NALWMSVQAE SLGPVFEFMP GYETFWSYVP HFVHSPFYVY AYAFGDGLVN
ALYAAYEEGL PDFQAKYFDL LAAGGSKHHS ELLAPFGLDA SDPAFWDKGL SMIEGFIDEL
EALEQQA
//
