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Database: UniProt
Entry: A0A2I0QZI7_9FLAO
LinkDB: A0A2I0QZI7_9FLAO
Original site: A0A2I0QZI7_9FLAO 
ID   A0A2I0QZI7_9FLAO        Unreviewed;       443 AA.
AC   A0A2I0QZI7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, 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:PKR79741.1};
GN   ORFNames=CW751_13530 {ECO:0000313|EMBL:PKR79741.1};
OS   Brumimicrobium salinarum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Crocinitomicaceae; Brumimicrobium.
OX   NCBI_TaxID=2058658 {ECO:0000313|EMBL:PKR79741.1, ECO:0000313|Proteomes:UP000236654};
RN   [1] {ECO:0000313|EMBL:PKR79741.1, ECO:0000313|Proteomes:UP000236654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHR20 {ECO:0000313|EMBL:PKR79741.1,
RC   ECO:0000313|Proteomes:UP000236654};
RA   Do Z.-J., Luo H.-R.;
RT   "The draft genome sequence of Brumimicrobium saltpan LHR20.";
RL   Submitted (DEC-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}.
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:PKR79741.1}.
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DR   EMBL; PJNI01000019; PKR79741.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0QZI7; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000236654; 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; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR   Gene3D; 2.30.42.10; -; 1.
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; 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:PKR79741.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236654};
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        103..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        375..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        413..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          10..427
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   443 AA;  49527 MW;  121DD1C9BA39600B CRC64;
     MDFWIKAAQL ILSLAILVTV HEFGHYLAAR AFKIRVEKFY LFFDPWFSLL KKKIGDTEWG
     IGWLPLGGYV KIAGMIDESM DTDQMAEPPK EDEFRSKPAW QRLIVMAAGV IVNVVVGIFI
     YIMVVAAWGD NVVSNDTLKY GVAVNKNFAE LNTGIEDGDV ITAVDGEAVE NVNLINFQIF
     LRGYRELEVQ QPSGEKKTIT LDKNVDDWMW ENDAVMAFSP RIPVVVDSVM ENRHAFIAGL
     QKGDSITTIN GVETPFFHDL QAELAKQEGD STAVKVGFYR GGSFQEISTF TDAKKTIGFI
     PKNPAWLKST HRSYTFGESI SRGIDKAIWT MHDYAAQLPL IFTSKGAQSV GGFGAIGSLF
     PPAWDWEVFW ARTAFISLIL AIMNILPIPA LDGGHIVFLL YEMITGKEAP QKVLEYAQLI
     GFLLLISLFL FANGNDVYRA FFK
//
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