ID A0A0X1TKC0_9FIRM Unreviewed; 564 AA.
AC A0A0X1TKC0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:AMC08495.1};
GN ORFNames=AT726_05870 {ECO:0000313|EMBL:AMC08495.1};
OS Turicibacter sp. H121.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Turicibacteraceae; Turicibacter.
OX NCBI_TaxID=1712675 {ECO:0000313|EMBL:AMC08495.1, ECO:0000313|Proteomes:UP000057144};
RN [1] {ECO:0000313|Proteomes:UP000057144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H121 {ECO:0000313|Proteomes:UP000057144};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMC08495.1, ECO:0000313|Proteomes:UP000057144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H121 {ECO:0000313|EMBL:AMC08495.1,
RC ECO:0000313|Proteomes:UP000057144};
RX PubMed=27013036;
RA Auchtung T.A., Holder M.E., Gesell J.R., Ajami N.J., Duarte R.T., Itoh K.,
RA Caspi R.R., Petrosino J.F., Horai R., Zarate-Blades C.R.;
RT "Complete Genome Sequence of Turicibacter sp. Strain H121, Isolated from
RT the Feces of a Contaminated Germ-Free Mouse.";
RL Genome Announc. 4:0-0(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013476; AMC08495.1; -; Genomic_DNA.
DR RefSeq; WP_068759225.1; NZ_JAMQUX010000069.1.
DR AlphaFoldDB; A0A0X1TKC0; -.
DR KEGG; tur:AT726_05870; -.
DR OrthoDB; 9762795at2; -.
DR Proteomes; UP000057144; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09606; M3B_PepF; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011976; Pept_M3B_oligopep-rel.
DR NCBIfam; TIGR02289; M3_not_pepF; 1.
DR PANTHER; PTHR11804:SF28; OLIGOENDOPEPTIDASE F; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000057144};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 167..544
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 564 AA; 66084 MW; 0EE55B4DAC6CD564 CRC64;
MKFSEFKYER PNFDQYKATM TSLIDQFKVA SSASEQLNIV TEINETRNHI ETMATLASIR
HSIDTRDEFY DAEQNYWDEY GPLYEEINSL FYDAVVSSPY RNELEEKLSK QFFTILDYRL
KAFSPEIIAD LQEENKLSSQ YTKLLASAKI PFDGEERTLP GMGKYLLSED RNVREAASKA
KYAFFEEHEA EIDEIYDQLV KVRTRIAKKL GFNNFVELGY VRMTRSDYNP EMVENFRKQV
LDYIVPVATS LYNRQEARLG YGTLRYFDEK FEFKTGNATP KGEPEWILEN GVKMYHELSP
QTKEFFDFMV DSELLDLVNK PGKAGGGYCT YIPEYKAPFI FSNFNGTAGD IDVLTHEAGH
AFQVYSSRWI ETPELNFPTY ESCEIHSMSM EFFTWPWMNL FFKEDTEKYK FTHLGSAIKF
IPYGIVVDAF QHFVYYNPDA TPAQRKSAWR ELEKQYLPHK NYEGCDFLER GGWWFQQSHI
FGSPFYYIDY TLAQICALQF WKRMHDNREE AWNDYVRLCE VGGTKSFLGL VEYANLKSPF
EDGCVSSIIT DIKAWLDAVE DQQL
//
