ID J9ZAL1_LEPFM Unreviewed; 243 AA.
AC J9ZAL1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Zn-dependent protease {ECO:0000313|EMBL:AFS53580.1};
GN OrderedLocusNames=LFML04_1356 {ECO:0000313|EMBL:AFS53580.1};
OS Leptospirillum ferriphilum (strain ML-04).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS53580.1, ECO:0000313|Proteomes:UP000006177};
RN [1] {ECO:0000313|EMBL:AFS53580.1, ECO:0000313|Proteomes:UP000006177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML-04 {ECO:0000313|EMBL:AFS53580.1,
RC ECO:0000313|Proteomes:UP000006177};
RX PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT its physiology and environmental adaptation.";
RL J. Microbiol. 49:890-901(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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DR EMBL; CP002919; AFS53580.1; -; Genomic_DNA.
DR RefSeq; WP_014961090.1; NC_018649.1.
DR AlphaFoldDB; J9ZAL1; -.
DR STRING; 1048260.LFML04_1356; -.
DR KEGG; lfi:LFML04_1356; -.
DR PATRIC; fig|1048260.3.peg.1470; -.
DR HOGENOM; CLU_086979_0_0_0; -.
DR Proteomes; UP000006177; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06158; S2P-M50_like_1; 1.
DR InterPro; IPR008915; Peptidase_M50.
DR InterPro; IPR044537; S2P-M50-like.
DR PANTHER; PTHR35864; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR PANTHER; PTHR35864:SF1; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AFS53580.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 65..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..202
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 243 AA; 26652 MW; DE5380581AD5900B CRC64;
MFHFDSGMAY LSETGFQITT VGIPLLLAVT LHEVAHGAVA DRLGDHTARY LGRLTLNPFP
HVDPFGTILL PLMLYFSHTG LMFGYAKPVP INPLNMANPR RDMAIVAMAG PLSNLLQALV
YMSLLHSFLG IVMTTSWFQS GEAGETVARL VITLFRMGIL VNVVLFVFNL IPLPPLDGGR
VLTGFLPAGG AAFMNRIEPW GMWILFGLIL LDPYLGVLSR LVWPEMDSLT NLLMVWATKP
GVS
//
