ID Q0EYG0_9PROT Unreviewed; 452 AA.
AC Q0EYG0;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SPV1_05709 {ECO:0000313|EMBL:EAU54232.1};
OS Mariprofundus ferrooxydans PV-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU54232.1, ECO:0000313|Proteomes:UP000005297};
RN [1] {ECO:0000313|EMBL:EAU54232.1, ECO:0000313|Proteomes:UP000005297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV-1 {ECO:0000313|EMBL:EAU54232.1,
RC ECO:0000313|Proteomes:UP000005297};
RA Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-2006) 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:EAU54232.1}.
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DR EMBL; AATS01000010; EAU54232.1; -; Genomic_DNA.
DR RefSeq; WP_009851435.1; NZ_DS022295.1.
DR AlphaFoldDB; Q0EYG0; -.
DR STRING; 314344.AL013_06085; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_0_1_0; -.
DR InParanoid; Q0EYG0; -.
DR OrthoDB; 5287739at2; -.
DR Proteomes; UP000005297; 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; 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:EAU54232.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005297};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 107..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 377..410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 422..443
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 131..194
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 200..263
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 452 AA; 49634 MW; 5D0CCF43E6663EB3 CRC64;
MIEILHTSLA FVVAIALLIA VHEYGHFTVA RRLGIRVEKF SIGFGPALFS WRSRDGEVLY
VIAAIPLGGY VKMLGENPDE QAEEFENKLS AEERARSFNL QPVWKRAAVA VAGPGFNFVF
AIFAFMLVAW LGQSVLPTIV GHIAPASIAE QAGLQVGDRI LAVNRSSVHS WQQMEEQLKD
HVGGQVQLRV QRDERPVTLD MTLPRQSTDP LMLNVADSVL GFDPGLTIKV DDVMSGSPAE
RAGLKPGDII RQIDGWPVAN VNQFIERIKA SAGHDVSVVV LRDQTLLQLQ VTPVSDDHQQ
VRIGVRLASH AMHKAELYRM GLFDGMSYGF VRTWQMTRMT LSVFGKMVTA AISPDNLGGP
IAIAQLAGRT ADLGLVYFIG FLALISVNLG VLNLLPVPIL DGGMLLYLGL EKLRGRALPP
KFLEITQMIG LMLIIGLMVF AFYNDISRLF RG
//
