ID A0A3N6ZVF0_9BACT Unreviewed; 456 AA.
AC A0A3N6ZVF0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN Name=rseP {ECO:0000313|EMBL:RQO32486.1};
GN ORFNames=DBR32_02470 {ECO:0000313|EMBL:RQO32486.1};
OS Taibaiella sp. KBW10.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Taibaiella.
OX NCBI_TaxID=2153357 {ECO:0000313|EMBL:RQO32486.1, ECO:0000313|Proteomes:UP000279469};
RN [1] {ECO:0000313|EMBL:RQO32486.1, ECO:0000313|Proteomes:UP000279469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBW10 {ECO:0000313|EMBL:RQO32486.1,
RC ECO:0000313|Proteomes:UP000279469};
RA Lee F., Williams K.B., Levin M., Wolfe B.E.;
RT "The microbiome of the planarian worm Dugesia japonica mediates outcomes of
RT regeneration via indole production.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU362031};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}.
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:RQO32486.1}.
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DR EMBL; QAJI01000001; RQO32486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6ZVF0; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000279469; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW Metal-binding {ECO:0000256|RuleBase:RU362031};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU362031};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:RQO32486.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000279469};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362031};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 112..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 427..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 11..442
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 231..283
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF17820"
SQ SEQUENCE 456 AA; 51326 MW; 81ACCE0AF2481CAA CRC64;
MSGLWVQIAQ FFVALSLLIV LHEGGHFFFA RLFKTRVEKF YLFFDFLFPF SNVLPFSLWK
KKKGDTEYGI GWFPLGGYVK IAGMVDESMD KEQMAKPPEP WEFRSKKPWQ RLLIMLGGII
VNILTAFLIY AMILFVWGEK KLPMSELRNG IEVADSLAYQ LGFKDGDIIK KVNSEDLVYY
NDLMPKMLYA QTVTVSRSGK DTTFGLPVNF VEQLVDNKSK MLFAVPFPAA IKEVTPDKNA
AKAGLLAQDK ILSVAGTPTH TVIEFKKALQ LHKGNIVPIS VERKGTITSL NTAIAADGTI
GIELNLPSNN EELAKMSNLK MEVKKYGFFE AIPAGMVMAK NKIGDYLGQF KLIFNPKTGA
YKGVGGFDSM RKIFPEEWHW QSFWNITAFI SLALAIMNLL PIPGLDGGYV MFTLWEMITG
RKPNEKFLEI VTTIGLVLLL ILMVAVNAND ILKYFK
//
