ID A0A1W2DIX7_9SPHI Unreviewed; 443 AA.
AC A0A1W2DIX7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SAMN04488101_1079 {ECO:0000313|EMBL:SMC96896.1};
OS Pedobacter nyackensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=475255 {ECO:0000313|EMBL:SMC96896.1, ECO:0000313|Proteomes:UP000192678};
RN [1] {ECO:0000313|EMBL:SMC96896.1, ECO:0000313|Proteomes:UP000192678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19625 {ECO:0000313|EMBL:SMC96896.1,
RC ECO:0000313|Proteomes:UP000192678};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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; FWYB01000007; SMC96896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2DIX7; -.
DR STRING; 475255.SAMN04488101_1079; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000192678; 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; PF13180; PDZ_2; 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.
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:SMC96896.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192678};
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 365..386
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 419..438
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 121..192
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT DOMAIN 210..280
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 443 AA; 48645 MW; C7269ECB63A6E507 CRC64;
MSGLIMAAQL LLGLSILVIL HELGHFLAAR AFGIKVEKFY LFFDAWGFKL FSFKKGDCEY
GIGWLPLGGY VKIAGMIDES MDTEQMNQPA QPWEFRSKPA WQRLIVMLGG VVVNIIVGIF
IFWMLTFKYG ETYIANSSVQ NGINPGSIGK EIGLQKGDRV IAVNGNKVIR FEELMSSKVL
LGNTSLTIVR GDKTMDIKVP DNILNKVSDL GIEAFISRAP LLTSTVDSII AGKAAFKAGL
QKGDRITAIN SVPVKYDADV RELIPKFKGK SVTFDVNRGA QHLTYTVPVD TAGTIGIGFN
INEIKEETIK YGLIAALPIG ANQAWKTFSD NAKGIWKVLT GKIQANKAFS GPVEIARKVY
GGEWIWARFW ASTGFISIAL AFMNLLPIPA LDGGHVVFLL VEMVKGKPLG DKFMERAQIA
GFVILLSLMV FVLGNDIFKA FFK
//