ID   A0A285J4H3_9GAMM        Unreviewed;       451 AA.
AC   A0A285J4H3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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   ORFNames=SAMN06297280_2808 {ECO:0000313|EMBL:SNY55225.1};
OS   Arsukibacterium tuosuense.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Arsukibacterium.
OX   NCBI_TaxID=1323745 {ECO:0000313|EMBL:SNY55225.1, ECO:0000313|Proteomes:UP000219353};
RN   [1] {ECO:0000313|EMBL:SNY55225.1, ECO:0000313|Proteomes:UP000219353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12461 {ECO:0000313|EMBL:SNY55225.1,
RC   ECO:0000313|Proteomes:UP000219353};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-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; OBEB01000006; SNY55225.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285J4H3; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000219353; 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.
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:SNY55225.1};
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..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        99..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        377..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        427..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          118..186
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   DOMAIN          211..280
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   451 AA;  49513 MW;  5C46435F73FA1180 CRC64;
     MAVFLWNAFT FVVALGLLVT VHEFGHFWVA RKNGVLVKRF SIGFGKALFS WRDRQGTEFV
     IAAIPLGGYV RMLDERIDPV LPQFADLAFN HKTVWQRMAI IAAGPAANFI FAIFILWLMY
     LIGVQEAKPV IAAVQPQSIV ADAGVQGNEQ IISINGHTAR DLRSTNLLLV EQLGRAQLTM
     GLEDINSGQQ RQVQLNLADW QFDPERQTVF ASLGIELMQP QRTTELAVVV PESAAERAGL
     QKGDIIKRID DELINDWPTL ERVIQQNAEQ TLQLEISRAG QNLQLTATPE LLTRDDGFSQ
     GMLGIQPVVT PWPEGIIYTQ RYGVFGAIGE GVGQTWQLTR LSFAMVAKLL TGDVSVKHLS
     GPISIAQGAG DTASMGLIAF LAFLALISVN LAVINLLPLP ILDGGHLMYL VVELIRGKPV
     SEKAQEIGFR FGALVLLMLM GIALLNDISR L
//