ID   I4BYR3_ACEMN            Unreviewed;       603 AA.
AC   I4BYR3;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   OrderedLocusNames=Anamo_1834 {ECO:0000313|EMBL:AFM22420.1};
OS   Acetomicrobium mobile (strain ATCC BAA-54 / DSM 13181 / JCM 12221 / NGA)
OS   (Anaerobaculum mobile).
OC   Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae;
OC   Acetomicrobium.
OX   NCBI_TaxID=891968 {ECO:0000313|EMBL:AFM22420.1, ECO:0000313|Proteomes:UP000006061};
RN   [1] {ECO:0000313|Proteomes:UP000006061}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-54 / DSM 13181 / NGA
RC   {ECO:0000313|Proteomes:UP000006061};
RX   PubMed=23961311; DOI=10.4056/sigs.3547050;
RA   Mavromatis K., Stackebrandt E., Held B., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Mikhailova N., Huntemann M., Pati A.,
RA   Chen A., Palaniappan K., Land M., Rohde M., Spring S., Goker M., Woyke T.,
RA   Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of the moderate thermophile Anaerobaculum mobile
RT   type strain (NGA(T)).";
RL   Stand. Genomic Sci. 8:47-57(2013).
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; CP003198; AFM22420.1; -; Genomic_DNA.
DR   RefSeq; WP_014807644.1; NC_018024.1.
DR   AlphaFoldDB; I4BYR3; -.
DR   STRING; 891968.Anamo_1834; -.
DR   KEGG; amo:Anamo_1834; -.
DR   PATRIC; fig|891968.3.peg.1820; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_0; -.
DR   Proteomes; UP000006061; 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:UP000006061};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          120..188
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          209..586
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   603 AA;  69372 MW;  11F08AFC0BDE669E CRC64;
     MSEKRSVTVP ERNEIEEKYK WRLEDLYPNN DAWGEEARCL ESAIENLKEM GTALTSSAQS
     LLRGLQTRDE IAERLGRLYA YASFKSHEDA RNLEAQAMVQ RASTVYLHFA EAVSSFVPCI
     LELGKEGIDE FMKEESGLEI YRVEIERIMR LKEHILSYEG EKLLAMSVDV GEVPEKVFSL
     LTNADMKFPK IKDEKGEEVE LSEERYSYFL HSSDRRVRRD AFKGLFSSYG NVKNTLSATY
     LGSLKKDVFY SKARKYENTL QASLYPQNIP IVVYEKAIET INQWLDPLRR YVTFKRKALN
     LDAMHFYDLY VQLLPEPKAH FSYDDAKSII IEGLAPLGEE YSRVLLEAFE NRWIDVYESK
     GKRSGAYSWG VYGVHPYVLL NFNGTLRDVF TLGHEMGHAM HSHFTFKSQP YVYSGVSIFT
     AEVASTTNEI LLLEHLIKRA ADKAEKAYLV NYGLEQVRTT VYRQLLFAEF ELEVHKRIEK
     GHPLTSEDFS AIWKSLYEKH YGDTLFIDEE LPLEWARIPH FYTAYYVYQY ATGYSAARAI
     ATAILSEGKP AVDRYLRFIS LGDSMDPVDA LKVAGVDMTS PRPLELTCKK FEEDLDVLMG
     LIG
//