ID A0A011RP60_9LACT Unreviewed; 602 AA.
AC A0A011RP60;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=ADIAL_0828 {ECO:0000313|EMBL:EXJ23713.1};
OS Alkalibacterium sp. AK22.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ23713.1, ECO:0000313|Proteomes:UP000020164};
RN [1] {ECO:0000313|EMBL:EXJ23713.1, ECO:0000313|Proteomes:UP000020164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA Singh A., Pinnaka A.K.;
RL Submitted (JAN-2014) 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:EXJ23713.1}.
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DR EMBL; JANL01000019; EXJ23713.1; -; Genomic_DNA.
DR RefSeq; WP_034300371.1; NZ_JANL01000019.1.
DR AlphaFoldDB; A0A011RP60; -.
DR PATRIC; fig|1229520.3.peg.825; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000020164; 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; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR004438; Peptidase_M3B.
DR NCBIfam; TIGR00181; pepF; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF45; SIMILAR TO OLIGOENDOPEPTIDASE; 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:UP000020164};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 118..178
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 201..582
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 602 AA; 68481 MW; 73E907BFBB7AFE02 CRC64;
MSEQLLKRSD VADELKWDLS AIFKTKEEFE EAAKQLPEDV AAFAGKYDGQ LTEAETVVEA
IAAYEELSAA ASHLGQYGHL PVSVDITDSE AQQVTRHVSN VLAGVSARLS FFQSQMEELD
EATLDAVKEQ EPAYAAYIRK IKKTKRAKLD PKVEEALAQL SPVFSSPAEI FEQARSNDAD
YGTFEVDGKE YPLSFVLYEE VYMYHEDPKV RRAAYDQFNS VLGQYKNVVA TAYYTHLQRE
KTIADMRGYD SIFDYLLESQ EVDQDLYHRQ IDTIMTDFAP VMRKFITHLK EVHGLEKMTY
ADLKVDLDPD YTLPVSIEES KTLVKEALEP LGQDYVDMIL RSYPERWVDF AQNLGKRSGA
FCSTTYGKHP NVMVTWTGQL TDAYTLFHEL GHAGQGVFSN ENNPLTSARP SLYLIEGPST
FNELLLTDYL KNKTDDPRME RSVLSKMISR TYFHNFVTHL LEAAYQREVY RLIDAGKSFD
ANKLSELKRE VLEQFWGEAV ELEPGAELTW MRQIHYYMGL YPYTYSAGLT IATQAFLKIS
SGEEKVDGWL DFLALGGQKE PAEATQVCGV DITTDKPLKD TINYLDESVD RIIELTKELD
QN
//
