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Database: UniProt
Entry: A0A1T5FUX1_9FLAO
LinkDB: A0A1T5FUX1_9FLAO
Original site: A0A1T5FUX1_9FLAO 
ID   A0A1T5FUX1_9FLAO        Unreviewed;       445 AA.
AC   A0A1T5FUX1;
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=SAMN05660477_02302 {ECO:0000313|EMBL:SKB99854.1};
OS   Soonwooa buanensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Soonwooa.
OX   NCBI_TaxID=619805 {ECO:0000313|EMBL:SKB99854.1, ECO:0000313|Proteomes:UP000191112};
RN   [1] {ECO:0000313|EMBL:SKB99854.1, ECO:0000313|Proteomes:UP000191112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22323 {ECO:0000313|EMBL:SKB99854.1,
RC   ECO:0000313|Proteomes:UP000191112};
RA   Peterson S.W.;
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; FUYZ01000008; SKB99854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5FUX1; -.
DR   STRING; 619805.SAMN05660477_02302; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000191112; 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:SKB99854.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191112};
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        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        102..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        417..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          190..275
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   445 AA;  50053 MW;  50DDBB64DE189B65 CRC64;
     MAPEQLFQFI LSISILVILH ELGHFIPAKL FKTKVEKFYL FFDPWFSIAK KKIGETEYGI
     GWLPFGGYVK IAGMVDESMD TDQLKKPAEP WEFRSKPAWQ RLIIMLGGVT VNFFLAWLIY
     SCLSYFKGEK YYDNAKFEAG IAVTSEGAKM GLKTGDKILK IDGKPAERMQ TSIMNMLFAN
     NVTVLRDGKE VTFPVNEDGV AEVLKANEAK LYFSNRFPAV VDSIAPNLPA AAMGLKKGDK
     IIEINNQPTQ YYDQVTTALL QNAGKPISVK VDRNNQVETL QTTLGKDGKL GFGINGALAQ
     KELDKTQVVK NYTFLESIPR GFERTIDVLV MQVKQFKIIF NSKTEGYKKV SGPIGIIKQM
     PETINWEFFW SFTAMFSVWL AFLNLIPIPG LDGGHVVFTL WEMITGKPVP QKVLENAQMI
     GVIFLLGLMV LIFGNDIVKW ITGKF
//
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