ID C4XE87_MYCFP Unreviewed; 608 AA.
AC C4XE87;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN OrderedLocusNames=MBIO_0194 {ECO:0000313|EMBL:BAH69459.1};
OS Mycoplasmopsis fermentans (strain ATCC 19989 / NBRC 14854 / NCTC 10117 /
OS PG18) (Mycoplasma fermentans).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC Mycoplasmopsis.
OX NCBI_TaxID=496833 {ECO:0000313|EMBL:BAH69459.1, ECO:0000313|Proteomes:UP000006810};
RN [1] {ECO:0000313|EMBL:BAH69459.1, ECO:0000313|Proteomes:UP000006810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18
RC {ECO:0000313|Proteomes:UP000006810};
RX PubMed=19219498; DOI=10.1007/s00284-009-9362-6;
RA Ishida N., Irikura D., Matsuda K., Sato S., Asano K.;
RT "Molecular cloning and expression of a novel cholinephosphotransferase
RT involved in glycoglycerophospholipid biosynthesis of Mycoplasma
RT fermentans.";
RL Curr. Microbiol. 58:535-540(2009).
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; AP009608; BAH69459.1; -; Genomic_DNA.
DR RefSeq; WP_013526687.1; NC_021002.1.
DR AlphaFoldDB; C4XE87; -.
DR KEGG; mfp:MBIO_0194; -.
DR PATRIC; fig|496833.3.peg.616; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_14; -.
DR Proteomes; UP000006810; 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 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:UP000006810};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 119..179
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 202..584
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 608 AA; 71790 MW; 921901138AFADE7E CRC64;
MKQYKNIKEV EEKYTFDLED ILKGQTIYDL FNEFIELSKI ALKTKDTKYE NVENYIKSVE
LGKDMGVLSN RIHNYLSNHS NQNLVDSKWT DLSTKWENIT NKISEEMGSE AVRFFKNIEK
LKIWKDDPRL KKERRGIIDA IEEYEHKLSD EVEEYLNQSS SANPDYESIF NIISDSELDY
GFATDSKGKK YKLSPAIKAK FMKKDDFKIR KSTRDSFLKA HMKHKDSMAN LLYQHFKGLT
VTAKIRKYKN TIDMLTHSDK VDDSMLQFLF DKVSTLKHTI KNRNKYYKKF YEAKFKEKYH
AKYDSYRELV KVKSTYTVEQ MQNIVSEALK PFGSEYHKMI TKAINERWVD YMTVDNKLSG
AYSIGNTYGL DKKYILMNFD GELGSVETLA HELGHSMHSY FSDKNNDISN ASYPIILAEI
ASIFNELMLY NYLLKTSKND LFKFKILDNM IDGFVGTVFR QILWANYEYD LYNAIEKDQA
SPSYTSLSKI YHKNSMKYAT KKIKYKKEKN IMSVYVPHYY YGFYVYKYAI GQLVANYFYT
RVKNEGEKYL QVYINDFLSA GDRDYPLETL KKVGADLKDP QFYEIGFSYF KEIVKEWIKL
GKKIFKVK
//
