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Database: UniProt
Entry: A0A1T5EX02_9SPHI
LinkDB: A0A1T5EX02_9SPHI
Original site: A0A1T5EX02_9SPHI 
ID   A0A1T5EX02_9SPHI        Unreviewed;       442 AA.
AC   A0A1T5EX02;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=SAMN05661099_3246 {ECO:0000313|EMBL:SKB88446.1};
OS   Daejeonella lutea.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Daejeonella.
OX   NCBI_TaxID=572036 {ECO:0000313|EMBL:SKB88446.1, ECO:0000313|Proteomes:UP000189981};
RN   [1] {ECO:0000313|Proteomes:UP000189981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22385 {ECO:0000313|Proteomes:UP000189981};
RA   Varghese N., Submissions S.;
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; FUYR01000005; SKB88446.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5EX02; -.
DR   STRING; 572036.SAMN05661099_3246; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000189981; 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; 2.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR001478; PDZ.
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   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
DR   PROSITE; PS50106; PDZ; 1.
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:SKB88446.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189981};
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        104..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        368..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        418..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          225..279
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   442 AA;  48190 MW;  D20A002EDB9C0841 CRC64;
     MDGLVMTGQL LLGLSILIIL HEAGHFLAAR AFGIRVEKFY LFFDAWGFKL VSFNYKGCEY
     GIGWLPLGGY VKISGMIDES MDTEQLSGPP QPWEFRSKPA WQRLIVMLGG VTVNIVLGIF
     IFWMLTLSNG ETFVPNDKIP YGIAPGIIGR EIGLQNGDRI TEVNGKPVKR FEELTSSKVL
     LGNTELTVKR GEETKNIHVP GDVLEKVSDL GIGQFVEPRV KISGISMVEP GGNAEKAGVK
     LGDSILAINN TPVTFYDEFK QIVVANKGKQ VAITVARDNK TVQIPTKVTP EGTVGVYIPL
     YHDIPLETVE YGFLESLPVG ASRAWGSFMD NAKGLGKVAS GQVKANKAFT GPIGIATMFG
     STVNWVKFWS LVGLLSMALA LMNLLPIPAL DGGHAIFLLI EMVKGKPLGD KFMERAQMVG
     FVILITLMVF VFGNDIIKHV IN
//
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