ID   A0A0N0K1P6_9PROT        Unreviewed;       398 AA.
AC   A0A0N0K1P6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Peptidase M48 {ECO:0000313|EMBL:KPF76648.1};
GN   ORFNames=IP88_06390 {ECO:0000313|EMBL:KPF76648.1};
OS   alpha proteobacterium AAP81b.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1523432 {ECO:0000313|EMBL:KPF76648.1, ECO:0000313|Proteomes:UP000037971};
RN   [1] {ECO:0000313|EMBL:KPF76648.1, ECO:0000313|Proteomes:UP000037971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP81b {ECO:0000313|EMBL:KPF76648.1,
RC   ECO:0000313|Proteomes:UP000037971};
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|RuleBase:RU003983};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC   -!- SIMILARITY: Belongs to the peptidase M48 family.
CC       {ECO:0000256|RuleBase:RU003983}.
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:KPF76648.1}.
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DR   EMBL; LJHX01000058; KPF76648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0K1P6; -.
DR   STRING; 1523432.IP88_06390; -.
DR   PATRIC; fig|1523432.3.peg.2508; -.
DR   OrthoDB; 9781930at2; -.
DR   Proteomes; UP000037971; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   InterPro; IPR032456; Peptidase_M48_N.
DR   PANTHER; PTHR10120; CAAX PRENYL PROTEASE 1; 1.
DR   PANTHER; PTHR10120:SF24; CAAX PRENYL PROTEASE 1 HOMOLOG; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   Pfam; PF16491; Peptidase_M48_N; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003983};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037971};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   TRANSMEM        32..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        304..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..179
FT                   /note="CAAX prenyl protease 1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16491"
FT   DOMAIN          185..383
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   398 AA;  43515 MW;  C391C8E605705DE1 CRC64;
     MAFDPELATR AWLATLSGPA RARSDAYFEG GYLLLFVDAA ITIAVTWATL RFGWAARLSA
     WAGRRRDGSA RRPAVHALRF LPAYILLTTL LTLPWAIWEQ FVREHDYGLS TQSFPAWAGE
     AAIAITINLV AVTLLFTGIH AAIRRAPRDW WLGATGITIA GLAFFILIAP VVVEPLFNRY
     TPLPAGPVRT AVLSMARANG IPAENVFVVD ASRQTTRISA NVAGLGATTR IALNDNLLKQ
     PPDEIRAVMA HEMGHYVLGH VTKLLVALAI LAALLFLFVA RALPALLARF GAGWGVARLD
     DPAIFAPVTI LLTIAFLALT PLFNTLIRTQ EIEADRFGLN VARAPEAFAS IAVKLGQYRK
     LEPGPWEEAV FYDHPSGRTR VLTAMRWKAE HLGQSDIR
//