ID A0A0D0RH60_9FIRM Unreviewed; 558 AA.
AC A0A0D0RH60;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:KIR03404.1};
GN ORFNames=P261_02219 {ECO:0000313|EMBL:KIR03404.1};
OS Lachnospiraceae bacterium TWA4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1392836 {ECO:0000313|EMBL:KIR03404.1, ECO:0000313|Proteomes:UP000032079};
RN [1] {ECO:0000313|EMBL:KIR03404.1, ECO:0000313|Proteomes:UP000032079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TWA4 {ECO:0000313|EMBL:KIR03404.1,
RC ECO:0000313|Proteomes:UP000032079};
RX PubMed=25495654;
RA Gagen E.J., Wang J., Padmanabha J., Liu J., de Carvalho I., Liu J.,
RA Webb R.I., Al Jassim R., Morrison M., Denman S.E., McSweeney C.S.;
RT "Investigation of a new acetogen isolated from an enrichment of the tammar
RT wallaby forestomach.";
RL BMC Microbiol. 14:314-314(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIR03404.1}.
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DR EMBL; JPZU01000001; KIR03404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0RH60; -.
DR STRING; 1392836.P261_02219; -.
DR MEROPS; M03.010; -.
DR PATRIC; fig|1392836.3.peg.2505; -.
DR OrthoDB; 9762795at2; -.
DR Proteomes; UP000032079; Unassembled WGS sequence.
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; 2.
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:UP000032079};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 166..269
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT DOMAIN 311..507
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 558 AA; 66005 MW; B37046B442A9DEC5 CRC64;
MKFSQMPYQR INMDAVEKGY KDIIERTKNA TSGEEQFEIH REYYKFIGDI ETNMVLAHIR
HDIDTTDEFY EKENDFYDEV APLITNLENE YLKVLYESPY RKVLEEKIGR VTFKNIELAL
KSFDEKLIPL MQEENALQSR YGKLIAVAKI PFDGEIYNLS LMTQFTTSDD RTIRKRAWKA
VSDYFLSVTD EIDEIYDKMV KNRTEQAHML GFENYIELGY YRMNRNCYDQ KMVENFRSQV
KKYFIPFATK LHKQRQKDIG VETLKYYDNG VFFTNGNPKP IGTPDEILAK GQAMYRELSP
ETGEFFDFMR ENELFDVLGR KTKRQGGYMT YLPNFKSPFI FANFNGTSGD VDVITHECGH
AFQGFLLRDE EIREYANITM ETAEIHSMSM EYFTYRWMDN FFGERGDDYR KMHFSDSSIF
VPYGCMVDEF QHLVYAKPEM TPAERKQVWA ELEKVYRPHL DYDNDPFFAN GGFWQRQSHI
FQCPFYYIDY VLASVCAMQF KVRMDEDFDA AWADYVKLCN LSARDFYINV IKEAGLKVPF
EDGCMEALVP KLEKKAFV
//
