ID Q2VHN7_9LACT Unreviewed; 601 AA.
AC Q2VHN7;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN Name=pepF1 {ECO:0000313|EMBL:ABA47373.1};
GN ORFNames=pSK11L_33 {ECO:0000313|EMBL:ABA47373.1};
OS Lactococcus lactis.
OG Plasmid pSK11L {ECO:0000313|EMBL:ABA47373.1}.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1358 {ECO:0000313|EMBL:ABA47373.1};
RN [1] {ECO:0000313|EMBL:ABA47373.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SK11 {ECO:0000313|EMBL:ABA47373.1};
RC PLASMID=pSK11L {ECO:0000313|EMBL:ABA47373.1};
RX PubMed=16332824; DOI=10.1128/AEM.71.12.8371-8382.2005;
RA Siezen R.J., Renckens B., van Swam I., Peters S., van Kranenburg R.,
RA Kleerebezem M., de Vos W.M.;
RT "Complete sequences of four plasmids of Lactococcus lactis subsp. cremoris
RT SK11 reveal extensive adaptation to the dairy environment.";
RL Appl. Environ. Microbiol. 71:8371-8382(2005).
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}.
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DR EMBL; DQ149244; ABA47373.1; -; Genomic_DNA.
DR RefSeq; WP_014567973.1; NC_017478.1.
DR RefSeq; YP_005863090.1; NC_017478.1.
DR MEROPS; M03.007; -.
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|RuleBase:RU368091, ECO:0000313|EMBL:ABA47373.1};
KW Metal-binding {ECO:0000256|RuleBase:RU368091};
KW Metalloprotease {ECO:0000256|RuleBase:RU368091};
KW Plasmid {ECO:0000313|EMBL:ABA47373.1};
KW Protease {ECO:0000256|RuleBase:RU368091};
KW Zinc {ECO:0000256|RuleBase:RU368091}.
SQ SEQUENCE 601 AA; 69863 MW; C0D9CA9C670A0FE8 CRC64;
MAKNRNEIPE KLTWDLTTIY KTDKEWEAEL TRIKSELSLV EETDPGHLLD SAESLLTITE
KMLSISQQVE KLYVYASMKN DQDTREAKYQ EYQSKATALY VKFGEVYAFY EPEFLKISKE
VYNKWLGELQ KLKNYDHMFE RLFAKKAHIL SQKEEKLLAA AGEIFESPSE TFEIFDNADI
KLPMVKNESD EMIQLTHGNY SSLMESKNRG VRKAAYKALY SNYEQYQHTY AKTLQTNVKV
HNLNAQIRSY DSARQAALAN NFVPEKVYDV LMEAIHQHLP LLHRYIELRK KILGITDLKM
YDIYTPLSNL DYKFNYEDGV KKAEEVLAIF GKEYKGKVKA AFEQRWIDVE ENIGKRSGAY
SGGSYDTNAF MLLNWQETLD DLFTLVHETG HSMHSAFTRE NQPYVYGNYP IFLAEIASTT
NENILTETLL KESKDDKERF ALLNHWLDSF RGTVFRQSQF AEFEQKIHEA DAAGEVLTSE
YLNSLYGEIN EKYYNLAVKE NPEIQYEWAR IPHFYYNFYV FQYATGFAAA TFLAEKVVHG
STEDRQKYLE YLKAGSSAYP LEVIAKAGVD MESTDYLDAA FELFENRLSE LEKLVEKGVH
L
//
