ID A0A0A2TXT6_9BACL Unreviewed; 564 AA.
AC A0A0A2TXT6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:KGP80494.1};
GN ORFNames=P364_0119285 {ECO:0000313|EMBL:KGP80494.1};
OS Paenibacillus sp. MAEPY2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1395587 {ECO:0000313|EMBL:KGP80494.1, ECO:0000313|Proteomes:UP000030061};
RN [1] {ECO:0000313|EMBL:KGP80494.1, ECO:0000313|Proteomes:UP000030061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAEPY2 {ECO:0000313|EMBL:KGP80494.1,
RC ECO:0000313|Proteomes:UP000030061};
RX PubMed=24526641;
RA Chua P., Yoo H.S., Gan H.M., Lee S.M.;
RT "Draft Genome Sequences of Two Cellulolytic Paenibacillus sp. Strains,
RT MAEPY1 and MAEPY2, from Malaysian Landfill Leachate.";
RL Genome Announc. 2:0-0(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:KGP80494.1}.
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DR EMBL; AWUK01000027; KGP80494.1; -; Genomic_DNA.
DR RefSeq; WP_024631844.1; NZ_AWUK01000027.1.
DR AlphaFoldDB; A0A0A2TXT6; -.
DR MEROPS; M03.010; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9762795at2; -.
DR Proteomes; UP000030061; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 168..269
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT DOMAIN 307..544
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 564 AA; 65762 MW; 3325517DC3950D1F CRC64;
MKFSEYTYTR PDLEQIKTSF RELLSGFEAA NTVEEQSGYM DKINALRSDF ETQAQLVYIR
HSIDTNDTFY KAENEFLDES SPIIQEYITD YYRALVNSKF RAELEQKWGS QLFQLADLSL
KTFSPEIIED LQKENKLSTE YNQLIASAKI PFEGEERTLP QLHPFELSTD RSMRERASEA
RYTFMAEHEA EFDRIYDELV KVRTQIAKKL GYPSYVELGY DRMNRTDYNA EMVSNFRAQV
RDYIVPVATK LRERQRSRID VDNLYYYDQG FSFKTGNPTP KGDADWIIDN GKKMYAELSP
ETDTFFQMMT DNELMDLVSK KDKQGGGYCT FLNDYKVPFI FSNFNGTSGD IDVLTHEAGH
AFQVYESRHF EVPEYNWPTY ESAEIHSMSM EFFTWPWMEL FFKEDTDKYK FDHLSSGLLF
IPYGVAVDEF QHFVYANPDA TPAERKQAWR NIEKTYLPHI NYKDNAYLEQ GGFWHKQGHI
FSSPFYYIDY TLAQICAFQF WKRSNQDMKS AWADYLTLCK AGGSLSFTGL VELAGLNSPF
EDGCVSSVIG DIEAWLDGVD DKAL
//
