ID A0A0S8ZDQ1_9PSED Unreviewed; 450 AA.
AC A0A0S8ZDQ1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=ASE98_22050 {ECO:0000313|EMBL:KQN51466.1};
OS Pseudomonas sp. Leaf48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736221 {ECO:0000313|EMBL:KQN51466.1, ECO:0000313|Proteomes:UP000051774};
RN [1] {ECO:0000313|EMBL:KQN51466.1, ECO:0000313|Proteomes:UP000051774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf48 {ECO:0000313|EMBL:KQN51466.1,
RC ECO:0000313|Proteomes:UP000051774};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN51466.1, ECO:0000313|Proteomes:UP000051774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf48 {ECO:0000313|EMBL:KQN51466.1,
RC ECO:0000313|Proteomes:UP000051774};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN51466.1}.
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DR EMBL; LMLH01000010; KQN51466.1; -; Genomic_DNA.
DR RefSeq; WP_060541033.1; NZ_LMLH01000010.1.
DR AlphaFoldDB; A0A0S8ZDQ1; -.
DR STRING; 1736221.ASE98_22050; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000051774; 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; 2.
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; 2.
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}; Protease {ECO:0000256|ARBA:ARBA00022670};
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 97..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 382..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 423..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 225..256
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 450 AA; 48461 MW; 484BEEDD554F0389 CRC64;
MSALYMIVGT LVALGVLVTF HEFGHFWVAR RCGVKVLRFS VGFGMPLLRW HDKQGTEFVV
AAIPLGGYVK MLDEREGEVP LDQIEQSFNR KSVRQRIAIV AAGPIANFLL ALVFFWALAM
LGSEQVRPVI GAVESGSIAA KAGLSPGQEI VAIDGEPTTG WAAVNLQLVR RLGESGSLQV
MVREQGSTAD SPRELALDKW LKGADEPDPI HSLGIRPWRP ALPPVLAELD PKGPAQAAGL
KTGDRLLALD GRPLEDWQQV VDTVRKQPDS KIMLRVERDG AQIDVPVTLA ARGESKAPSG
YLGAGVKAVD WPPEMVREVS YGPLAAIGEG ARRTWTMSVL TLDSLKKMLF GELSVKNLSG
PITIAKVAGA SAQSGVADFL NFLAYLSISL GVLNLLPIPV LDGGHLLFYL IEWARGRPLS
DRVQGWGIQI GISLVIGVML LALVNDLGRL
//