ID   A0A1N7MHE7_9RHOB        Unreviewed;       607 AA.
AC   A0A1N7MHE7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:SIS85503.1};
GN   ORFNames=SAMN05421795_107129 {ECO:0000313|EMBL:SIS85503.1};
OS   Phaeovulum vinaykumarii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Phaeovulum.
OX   NCBI_TaxID=407234 {ECO:0000313|EMBL:SIS85503.1, ECO:0000313|Proteomes:UP000186098};
RN   [1] {ECO:0000313|Proteomes:UP000186098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18714 {ECO:0000313|Proteomes:UP000186098};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-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; FTOM01000007; SIS85503.1; -; Genomic_DNA.
DR   RefSeq; WP_076366869.1; NZ_OBMN01000007.1.
DR   AlphaFoldDB; A0A1N7MHE7; -.
DR   STRING; 407234.SAMN05421795_107129; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000186098; 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; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011977; Pept_M3B_clade3.
DR   NCBIfam; TIGR02290; M3_fam_3; 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|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186098};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          129..197
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          352..592
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   607 AA;  68156 MW;  97FA6A6BBD1D0D26 CRC64;
     MPHLPPRPLS DANASAAGEG LGPLPEWDLS DLYSAPDAPE LERDMAWLET ACAEFARDYE
     GKLADLDAAG MADCITRHEA IENISGRIFS YLGLRYYQNT LDGARTKALS DAQDRITAAT
     TPLVFFSLEF NRIPDDAYAA LFADARVARW KPVFDRMRAM RPHQLSDELE RFLHDQSVVG
     AAAWNRLFDE TMASLEFDVE GESKTLEATL DMLSDHDRSR RETGARALAQ VFGRNIKLFA
     RITNTLAKEK AIEDRWRKMP TPQHARHLSN HVEPEVVAAL RDAVVAAYPR LSHRYYRIKA
     RWMGLEKLQV WDRNAPLPTE TPRTIGWDEA RETVLGAYGA FSPRMAEIAQ PFFDKGWIDA
     AVKPGKAPGA FAHPTVTDVH PYVLLNYLGK PRDVMTLAHE LGHGVHQVLA APQGELLAST
     PLTLAETASV FGEMLTFRRL LDGAQTKAER RTLLAGKVED MINTVVRQIA FYDFECRVHA
     ARAKGELTPE EINAIWMQIQ HESLGDAFEF MPGYETFWTY IPHFIHSPFY VYAYAFGDGL
     VNALYAAYAE GLPDFQAKYF DMLSAGGARH HRELLAPFGL DASDPAFWMK GLSMIEGFIN
     ELETLED
//