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Database: UniProt
Entry: A0A1I5FUX5_9RHOB
LinkDB: A0A1I5FUX5_9RHOB
Original site: A0A1I5FUX5_9RHOB 
ID   A0A1I5FUX5_9RHOB        Unreviewed;       443 AA.
AC   A0A1I5FUX5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:SFO27598.1};
GN   ORFNames=SAMN04487859_12232 {ECO:0000313|EMBL:SFO27598.1};
OS   Roseovarius lutimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1005928 {ECO:0000313|EMBL:SFO27598.1, ECO:0000313|Proteomes:UP000198599};
RN   [1] {ECO:0000313|EMBL:SFO27598.1, ECO:0000313|Proteomes:UP000198599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28463 {ECO:0000313|EMBL:SFO27598.1,
RC   ECO:0000313|Proteomes:UP000198599};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; FOVP01000022; SFO27598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5FUX5; -.
DR   STRING; 1005928.SAMN04487859_12232; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000198599; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SFO27598.1};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..443
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011728088"
FT   DOMAIN          35..180
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          190..372
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   443 AA;  48951 MW;  1BB54889D6E0E86A CRC64;
     MRSLFVSFLL AITPLAPAMA EGQVTSFTLE NGLEVVVIED HRAPVVTQMV WYRAGSADEP
     PGASGVAHFL EHLLFKGTKT LEPGEFSATV SRNGGSDNAF TSYDYTAYFQ RIAADRLELM
     MRMESDRMVN LQLGEGDIAT ERDVIIEERN QRVENNPAAL FREQKNAAQY LNHHYGVPII
     GWQHEMYDLG LEDALAYYRT YYAPNNAILV IAGDVTPEDV RKLAETYYGP LPANPDLPER
     ARAQEPRQMA ERRMTFRDAR VAQPYLSRSY LAPERDSGAQ EEAAALTLLA EILGGGSTSV
     LTEKLQFDSR IAVQTGVYYS GLSLDDTTFS LVVVPAAGVT LEQAEAAMDD VLTGFLETGI
     DADQLARIKM QMRAAEIYAR DDAGGLANRY GRALTQGLNV ADVQAWPEIL QNTTEDDIMT
     AARKVFDRNT SVTGWLVAPE VTQ
//
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