ID   A0A2R8ABS8_9RHOB        Unreviewed;       388 AA.
AC   A0A2R8ABS8;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Metalloprotease LoiP {ECO:0000313|EMBL:SPF29674.1};
DE            EC=3.4.24.- {ECO:0000313|EMBL:SPF29674.1};
GN   Name=loiP_2 {ECO:0000313|EMBL:SPF29674.1};
GN   ORFNames=POI8812_01990 {ECO:0000313|EMBL:SPF29674.1};
OS   Pontivivens insulae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pontivivens.
OX   NCBI_TaxID=1639689 {ECO:0000313|EMBL:SPF29674.1, ECO:0000313|Proteomes:UP000244932};
RN   [1] {ECO:0000313|EMBL:SPF29674.1, ECO:0000313|Proteomes:UP000244932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CeCT 8812 {ECO:0000313|EMBL:SPF29674.1,
RC   ECO:0000313|Proteomes:UP000244932};
RA   Keele B.F.;
RL   Submitted (MAR-2018) 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}.
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DR   EMBL; OMKW01000002; SPF29674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8ABS8; -.
DR   OrthoDB; 9810445at2; -.
DR   Proteomes; UP000244932; 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   CDD; cd07332; M48C_Oma1_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR22726:SF25; BETA-BARREL ASSEMBLY-ENHANCING PROTEASE; 1.
DR   PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR   Pfam; PF01435; Peptidase_M48; 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:UP000244932};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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        95..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          168..340
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   388 AA;  41595 MW;  23ACA31EC6BDF6F9 CRC64;
     MVRGHYSDGQ TAASHEVTLH VHGGNLVIAA VDGDVLACWP VTELRQMQVS GAGGARVLGR
     MDDDARVSFH DRGLLDLISI YAPDMKKGLH KRQKFGPVLL ALAGAAIAFP LIFFVLLPRM
     AETLAVFITP ETEVAMGDRT YPQLVRVLSL GDEEALNRCV APEGSAVLAD MTTRMEERLD
     LPFPLRVEVW DHPLVNALAM PGGRIVLFRG FLEEVTGPDA VAGVLAHEIG HVANRDSVRL
     GLRAAGSAGV LGLVLGDFAG GAAALAIAEA MLSASYTREA ETAADEFALD QLAALDIPAI
     GMAEFFEELA PDEPHDHPGA LSHFATHPDI QGRAENARAR STGLTPALPD EDWAAMLAIC
     DQTEAILAED DWGQRFEDIF KSDDVEKE
//