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Database: UniProt
Entry: M6R5X4_LEPIR
LinkDB: M6R5X4_LEPIR
Original site: M6R5X4_LEPIR 
ID   M6R5X4_LEPIR            Unreviewed;       800 AA.
AC   M6R5X4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Thermolysin metallopeptidase, alpha-helical domain protein {ECO:0000313|EMBL:EMO03527.1};
GN   ORFNames=LEP1GSC116_1186 {ECO:0000313|EMBL:EMO03527.1};
OS   Leptospira interrogans serovar Icterohaemorrhagiae str. Verdun HP.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049910 {ECO:0000313|EMBL:EMO03527.1, ECO:0000313|Proteomes:UP000012092};
RN   [1] {ECO:0000313|EMBL:EMO03527.1, ECO:0000313|Proteomes:UP000012092}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Verdun HP {ECO:0000313|EMBL:EMO03527.1,
RC   ECO:0000313|Proteomes:UP000012092};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA   Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL   Submitted (JAN-2013) 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 M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388}.
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:EMO03527.1}.
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DR   EMBL; AHNZ02000836; EMO03527.1; -; Genomic_DNA.
DR   AlphaFoldDB; M6R5X4; -.
DR   Proteomes; UP000012092; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.490; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR045474; GEVED.
DR   InterPro; IPR025711; PepSY.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF20009; GEVED; 1.
DR   Pfam; PF03413; PepSY; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
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};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          109..147
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          160..251
FT                   /note="PepSY"
FT                   /evidence="ECO:0000259|Pfam:PF03413"
FT   DOMAIN          292..415
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          467..637
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   DOMAIN          710..793
FT                   /note="GEVED"
FT                   /evidence="ECO:0000259|Pfam:PF20009"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        549
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   800 AA;  90405 MW;  CB22660A0DAFF73D CRC64;
     MKYKQKFGFE KVKIFFLYLV VFLNFFLQGC KDGGGSTFGV EYWLGMLNSV PMDPKAVMES
     QLSSNGTINF VRFNSDLVPY SRSQASEVLK TYLQIPTEYT PKLVRSNESN GQVLDRFQQY
     YKGIKVENKI YTVVSKDNRI EFMGGDFSGI EQDLNITPNL SKEDALSKAL VHFGAKKYLW
     ESPEREDRLR SIKGDSKATY FPKGELIVYN RAESNLKNEY RLTYKFGISS LEPPSSKYVY
     VDARSGEILA SRDARRFETQ PGDGGGGTTP LPPPTDLGIC FPDPTPCIKN ATAKTRFSGY
     KTITTWTARE ENHYELKDYS RGKGIITYSW EFVDLGILGV QLQNIPMIDS DNYWSASEYH
     DDYNHDAVLD AHWGAEKTYD YFKTVHNHSG YDRDGAKVIG NVHAYGFANN AHWDPITEEI
     YYYYCPPESL CATVYTSPGQ IDPQYDDTTS LDFVSHEFGH GLSAYTSELG YSRGPGALNE
     GFSDIWNIVV NHYVNKIHAM NKNIWLFGDE TRPSGGIRSA SNPKSTTVKY PGPNTYKGEL
     WDFSDVDVHR NSNVLSHWFY ILSNGKQGIN DIWCEYNTSG ISIEKAEKIA YSSSLYLWPT
     AEYPDVRSAS IMASKYLYGS FSQEVKSTID AWDAVGVPAN TSSRGGAGMK PDYYITSVKL
     SEMERNSEND CGYKDSTYLN QTIYKGFTYT IRLSSRGDSI INMPSRTHKW RVWIDFDRNG
     TFNNSVNSTE LVAEGTISSY NGGIIQKTFT IPADALTGTT RMRVSMKAAT GAETYPRPDE
     KFIQGEVEDY MVTIRPFIVL
//
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