ID D2Z805_9BACT Unreviewed; 600 AA.
AC D2Z805;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=Dpep_1576 {ECO:0000313|EMBL:EFC91602.1};
OS Dethiosulfovibrio peptidovorans DSM 11002.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC91602.1, ECO:0000313|Proteomes:UP000006427};
RN [1] {ECO:0000313|EMBL:EFC91602.1, ECO:0000313|Proteomes:UP000006427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC91602.1,
RC ECO:0000313|Proteomes:UP000006427};
RX PubMed=21304695;
RA Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT strain (SEBR 4207).";
RL Stand. Genomic Sci. 3:85-92(2010).
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:EFC91602.1}.
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DR EMBL; ABTR02000001; EFC91602.1; -; Genomic_DNA.
DR RefSeq; WP_005661094.1; NZ_ABTR02000001.1.
DR AlphaFoldDB; D2Z805; -.
DR STRING; 469381.Dpep_1576; -.
DR PaxDb; 469381-Dpep_1576; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000006427; 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 Reference proteome {ECO:0000313|Proteomes:UP000006427};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 118..187
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 208..586
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 600 AA; 67743 MW; 4C519C28F169F1B3 CRC64;
MASDSRSIPV RSEIDESYKW DLSSIYGGIE EWENAWREVF ESVDTLESFS GKLGDGASCL
LGCLKEIDRV SLELGRVFVY ATMKSHEDAS DGEAKAMADR AMALNVRVST ALAYVLPEIL
GIEESRLASF FDDLPELEMY RYHIEQIIRK KAHVLSAREE ELLSGMGEIA NAPELIFSML
TNGDMKFPSI RDERGEAVEL SEERYYRLIR SKDRPVRERA FKGIHDTYES FRNTLAASFG
SAVKESVFDA RVHRYGSSRE AALDGGDIPL SVYDNLIKAV REGLPLLHDY VSLRKSSLGL
DELHMYDLYV PIVEEPEEDI SWEDAKKTVL AGLSPLGDGY LDVLKEGFDG RWVDVYESQG
KRKGAYSWGS YGTNPFVLLN YNGTLRDVFT LAHEMGHALH SWHSHKFQPP VYGDYTIFVA
EVASTTNEVL LMEHMLENRP KDRPFLLNYY LEQVRTTVFR QTMFAEFELK VHGMAEEGTP
LTPEILSSIW GDLNRDYYGP DIVVDKGIEV EWARIPHFYS PFYVYQYATG YSAATALAEG
ILTGGESARD RYIDFLKGGS SKSSIDLLRG AGVDMTSPDP VRSALRLFGE KIEELREITG
//
