ID W1Q1Z6_ABIDE Unreviewed; 605 AA.
AC W1Q1Z6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=GCWU000182_001596 {ECO:0000313|EMBL:ESK65053.1};
OS Abiotrophia defectiva ATCC 49176.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Abiotrophia.
OX NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK65053.1, ECO:0000313|Proteomes:UP000019050};
RN [1] {ECO:0000313|EMBL:ESK65053.1, ECO:0000313|Proteomes:UP000019050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK65053.1,
RC ECO:0000313|Proteomes:UP000019050};
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., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2013) 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:ESK65053.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACIN03000014; ESK65053.1; -; Genomic_DNA.
DR AlphaFoldDB; W1Q1Z6; -.
DR STRING; 592010.GCWU000182_001596; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_1_1_9; -.
DR Proteomes; UP000019050; 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; cd09609; 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; IPR034009; M3B_PepF_4.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR004438; Peptidase_M3B.
DR NCBIfam; TIGR00181; pepF; 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|RuleBase:RU368091};
KW Metal-binding {ECO:0000256|RuleBase:RU368091};
KW Metalloprotease {ECO:0000256|RuleBase:RU368091};
KW Protease {ECO:0000256|RuleBase:RU368091};
KW Reference proteome {ECO:0000313|Proteomes:UP000019050};
KW Zinc {ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 121..189
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"
FT COILED 32..59
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 605 AA; 68157 MW; CB56FBCF17E4E8FC CRC64;
MQNKEESKMS LPLRQELPLA ETWDLSLLYK DQAAYEVAVE DLKKQVTEFE ANYAGTLDQT
QQLEKALADY EAIQVAISWV SHYGSLAYET DKLDAQNEAN AVGLDQLFEL VGAKLAFLAP
ELSALDEAYL REFSQSDKGK RYAGYLNEVL RLKPSVLSKE VEELLSSFQS SLYNQYSLYG
TLKFQDLTFD DFQVAGKTYP NSFVKFEGDY EGASDYELRH ASWKSFHDGL ARYQHTAAAN
YLNYVQTSKK EAKLRGFDSI IDYELFKQDV SREAYNRQID VIMSEFAPVM RRYARLLAAE
QGLDKVSLAD IKMPFSKEPA ETISIEASRA MVEDTFKVLG PDYQEIVRRA FDERWIDYPM
NQTKSTGGFC ATVANGPSYI LLNWTGLLSE VLVLAHELGH AGHFQLTNQH VSPITPEASL
YFIEAPSTAN EVIMCQYLLS QPLEAAQKRT LIAEFIARTY FHNMVTHLLE AHFQRKVLEA
VDRDDFLNTD SLNQFFLETL KEFWGDALEI NPGAELTWMR QPHYFMALYP YTYSAGLTIG
TAVGQKIAAG DQTTIDKWLE VLKAGGTMGP LALAEHAGVS MADAGALRSA IGYVDHLLDQ
IEALA
//
