ID B0SPD4_LEPBP Unreviewed; 514 AA.
AC B0SPD4;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Putative metalloendopeptidase {ECO:0000313|EMBL:ABZ97458.1};
GN OrderedLocusNames=LEPBI_I1348 {ECO:0000313|EMBL:ABZ97458.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97458.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ97458.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP000786; ABZ97458.1; -; Genomic_DNA.
DR RefSeq; WP_012388339.1; NC_010602.1.
DR AlphaFoldDB; B0SPD4; -.
DR STRING; 456481.LEPBI_I1348; -.
DR KEGG; lbi:LEPBI_I1348; -.
DR HOGENOM; CLU_009902_1_2_12; -.
DR OrthoDB; 9811314at2; -.
DR BioCyc; LBIF456481:LEPBI_RS06610-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:InterPro.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..514
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002755496"
FT DOMAIN 48..95
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 268..444
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 514 AA; 59724 MW; 8ADEC3711313703D CRC64;
MMSKLRIFFL CFFLQFLPLF SEDAFFGTSE SQFREKIKTI QLENGLKVVM MKRGTSPTVA
LYIKFLVGAV DETPEEAGTA HLLEHMLFKG TQSVGTLDYK KEEKYQKQIE VWGTELDDLK
LQRRDLITRG ENVPKTLEEK IETLNRRLLN LIQLQDEFIV KNEDSYIYEQ NGEMGFNAYT
SQDVTNYQIQ LPNNRMEIWA KIESDRLKHP ILREYYTERD VVIEERRMRT DDVGGAVLRE
KFFSLAFESH PYRKPIIGYS AEIPYLKIEE TKAFFEKHYT PNRMVISIVG QFDMVETESI
VRKYFSDLKP GKPRPSYKIE EKSFPGEKRF KVLHPSASQM MMGWIKPPYP HKDNSSFDVL
SSILTSGTGS RLYKRLVLEE KLVLNIGAAN GYPGERYKNA FVFFISPNEG VDPKKIEAII
WEELNRIKEQ GIPNEELEKI KNQMVSDFMK TLDQNGAIAD LLSYYQLLYG DWAGLFQQYQ
TIMNTSSSDI QALIPKYLTK DLVIVGVLED GRKK
//
