ID A8MF43_ALKOO Unreviewed; 608 AA.
AC A8MF43;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN OrderedLocusNames=Clos_1166 {ECO:0000313|EMBL:ABW18712.1};
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688 {ECO:0000313|EMBL:ABW18712.1, ECO:0000313|Proteomes:UP000000269};
RN [1] {ECO:0000313|EMBL:ABW18712.1, ECO:0000313|Proteomes:UP000000269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs {ECO:0000313|EMBL:ABW18712.1,
RC ECO:0000313|Proteomes:UP000000269};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs {ECO:0000313|Proteomes:UP000000269};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) 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}.
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DR EMBL; CP000853; ABW18712.1; -; Genomic_DNA.
DR RefSeq; WP_012159024.1; NC_009922.1.
DR AlphaFoldDB; A8MF43; -.
DR STRING; 350688.Clos_1166; -.
DR KEGG; aoe:Clos_1166; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_9; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000000269; Chromosome.
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:UP000000269};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 121..190
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 211..591
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 608 AA; 70586 MW; B3AAC85F3727EF7A CRC64;
MASENKKQKV SSLERNEIDK AFKWDIEKMY QNEALWKKDY DTVKELIAEF VQYKGKLKDC
KNLLKALSLY ETLVEKTNKL YVYATMKRDE DNRNAKHQGL ADNAQSLYTR MGSSVAFFVP
EILSISEEDI QEFYRKETGL KKYQHYLDEI LRHKSHVLSA AEEEIVAQAG EVANGPRDIF
TMLNNADMKF PTIIDQSGVE VEVTHGNFIQ LLENPDRRVR EDAFSALYST YESYKNTLAT
VFSSSLKKDN FLAKVKKHKN SMSAALFNTN IPEEVYHNLI GVIHNHLHLM HRYVNLRKRM
LGLDELHMYD LYTPMVQNID MQIPYEEAKE LLVKGLSPLG EAYTNILKSG FRDRWVDVYE
NTGKTSGAYS WGTYDSYPFI LMSYKDNVNS MFTLAHEMGH SIHSYYTCKN QPFIYSDYKT
FVAEVASTVN EALLMDYMLK NTKETNERMY LLNYYLEQFR TTVYRQTMFA EFEKITHEKI
SMGEALTAED LNKIYRDLNI KYYGNDIIVD SHIDIEWARI PHFYNSFYVF QYATGYSAAI
ALSKKILMEG ENAVQQYIEF LKSGSSDYSI NVLKNAGVDM SSPAPIESAL KVFEDLLTEM
EEIAFKTK
//
