ID A0A0G0KKA9_9BACT Unreviewed; 590 AA.
AC A0A0G0KKA9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=PepF/M3 family oligoendopeptidase {ECO:0000313|EMBL:KKQ75945.1};
GN ORFNames=US96_C0001G0021 {ECO:0000313|EMBL:KKQ75945.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_38_5b.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618569 {ECO:0000313|EMBL:KKQ75945.1, ECO:0000313|Proteomes:UP000034181};
RN [1] {ECO:0000313|EMBL:KKQ75945.1, ECO:0000313|Proteomes:UP000034181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKQ75945.1}.
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; LBUZ01000001; KKQ75945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0KKA9; -.
DR Proteomes; UP000034181; 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; cd09610; 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 PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 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: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 113..181
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 197..577
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 590 AA; 69313 MW; 58C9ADCD06B177FB CRC64;
MAKNQPPKWD LRDFYKNTND SQIQKDQKLI KKLASDFIKK YKGKINSPKL TPDLLLSSLK
DIERLDETLY ILQNYAYYLH AQDSKDSKIG QFYQQIEEFG NKSTSELLWF LLEWQKLDNK
HAQKLLKGPL LSTYKHFLSH ARAFTPFRVS EAEEIILTKK SMAGSQAFIR LYDETSSQER
FALGKQRLTM SQLSPILKSH PSRSTRKQAS EVLTQVLKKH SHFYTFTLNN LLLDKKINDE
IRGYDYPQQA TFLSYEMEPK VVETMTKVIE QRYDISERFY KTKAKLLKQK LFEWDRYSVL
YPNDKIEYSW EEAKEMILKS FKQFSPVFYE TALKFFDNGW IDALITPNKR GGGFCSYSVP
AKHPMILVNF AGTHDDVSTL AHELGHGIHA YLSRGNTLNN YYPSTATAEI ASIFCENILF
DQVYSQITDK KVKLNMLANK IQGGLATIFR QNAFYLFEND IHNHRRQKGE LATSDINNYW
QHRLQPMFGK SLTLTQNHEY WWMYVLHFYH YNFYVFTYAF GEALTNSLYE MYRENPKTFV
PKYLDALTKG GSQNPKEILS SFDVDLNSSD FWNKSLNLLE EYVEDFEKLV
//