ID   A0A1V1ZI08_9FLAO        Unreviewed;       257 AA.
AC   A0A1V1ZI08;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Peptidase M48 Ste24p {ECO:0000313|EMBL:OMP31724.1};
GN   ORFNames=BKM32_01265 {ECO:0000313|EMBL:OMP31724.1};
OS   Mangrovimonas sp. DI 80.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mangrovimonas.
OX   NCBI_TaxID=1779330 {ECO:0000313|EMBL:OMP31724.1, ECO:0000313|Proteomes:UP000188854};
RN   [1] {ECO:0000313|EMBL:OMP31724.1, ECO:0000313|Proteomes:UP000188854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI 80 {ECO:0000313|EMBL:OMP31724.1,
RC   ECO:0000313|Proteomes:UP000188854};
RA   Krishnamurthi S., Pal Y., Verma A., Sundharam S.;
RT   "Taxonomic characterization of strain DI 80 closely related to
RT   Mangrovimonas sp.";
RL   Submitted (DEC-2016) 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:OMP31724.1}.
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DR   EMBL; MSDT01000002; OMP31724.1; -; Genomic_DNA.
DR   RefSeq; WP_076662215.1; NZ_MSDT01000002.1.
DR   AlphaFoldDB; A0A1V1ZI08; -.
DR   Proteomes; UP000188854; Unassembled WGS sequence.
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   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   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:UP000188854};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..257
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013115628"
FT   DOMAIN          72..247
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   257 AA;  28200 MW;  AF91F8A1B8636D71 CRC64;
     MRTNRFKIRL LLGLCIVAFA FIKRCSSMET NPYTGKDQVI NMTADQEIAI GLQSAPEMEQ
     QFGGLHPNNQ YQAFVTQVGN KLVQSSIASQ TPYDYHFHLL GDSNTVNAFA LPGGQVFITY
     ALFSQLENEA QLAGVLGHEI GHVLGRHSAE RIAETEFWKT VTTGASVGAD MGQLIGGIGQ
     QKLLTNSRGD ELEADDLGIM LMIDAGYEPE EMIGVMEILK AAAGPNRVPE YQSTHPDPDN
     RIEKIKAAID KYKKTPI
//