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Database: UniProt
Entry: A0A0N1AB04_9PROT
LinkDB: A0A0N1AB04_9PROT
Original site: A0A0N1AB04_9PROT 
ID   A0A0N1AB04_9PROT        Unreviewed;       456 AA.
AC   A0A0N1AB04;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=IP80_17260 {ECO:0000313|EMBL:KPF44823.1};
OS   beta proteobacterium AAP65.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF44823.1, ECO:0000313|Proteomes:UP000037849};
RN   [1] {ECO:0000313|EMBL:KPF44823.1, ECO:0000313|Proteomes:UP000037849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP65 {ECO:0000313|EMBL:KPF44823.1,
RC   ECO:0000313|Proteomes:UP000037849};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-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:KPF44823.1}.
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DR   EMBL; LJHW01000037; KPF44823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1AB04; -.
DR   STRING; 1523424.IP80_17260; -.
DR   PATRIC; fig|1523424.3.peg.2549; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000037849; 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; 1.
DR   Gene3D; 2.30.42.10; -; 2.
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   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:KPF44823.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037849};
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        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        434..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          7..439
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
FT   DOMAIN          230..269
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|Pfam:PF17820"
SQ   SEQUENCE   456 AA;  48889 MW;  F165DC759A299FD9 CRC64;
     MITTVLAFLL TLGILVVIHE YGHYRVAVAC GVKVLRFSVG FGQVIWRRQS APDATEFVLC
     ALPLGGYVRM LDEREAPVAP GQVNQAFNRK PLWQRAAIVS AGPLANLALA VLLYAAAHWI
     GVQEPKALIG PPAAGSVAER AGLRAGQWVQ AMDHGSGEWQ ELRSLTDLRW EVTQAALRGE
     RVRLQVSDGD GRAARSVDLD LSGIEAREVD AALTQRIGLG SPWREPVLGQ VQAGSAGAAA
     GLQRGDRVLS IDGQAVADAQ QVVEKVRGNL RAGQVSTQAW LVERDGRTLV LNVTPQVVTE
     KGQTFARVGV EPGRAPVMLT VQHGVFEGLQ LGAVRTWEVS VLTVKMLGRM LIGEASLKNL
     SGPLTIADYA GQSVTKGLAY YLGFLALVSV SLGVLNLLPL PMLDGGHLMY YIFEGVTGRP
     VSDLWLARLQ RGGIAVLLMM MSVALFNDVA RLLGLH
//
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