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Database: UniProt
Entry: A0A1H8BEJ6_9BACL
LinkDB: A0A1H8BEJ6_9BACL
Original site: A0A1H8BEJ6_9BACL 
ID   A0A1H8BEJ6_9BACL        Unreviewed;       535 AA.
AC   A0A1H8BEJ6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=SAMN05444955_102148 {ECO:0000313|EMBL:SEM81361.1};
OS   Lihuaxuella thermophila.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Lihuaxuella.
OX   NCBI_TaxID=1173111 {ECO:0000313|EMBL:SEM81361.1, ECO:0000313|Proteomes:UP000199695};
RN   [1] {ECO:0000313|EMBL:SEM81361.1, ECO:0000313|Proteomes:UP000199695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46701 {ECO:0000313|EMBL:SEM81361.1,
RC   ECO:0000313|Proteomes:UP000199695};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC       {ECO:0000256|RuleBase:RU366073}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU366073};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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DR   EMBL; FOCQ01000002; SEM81361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8BEJ6; -.
DR   STRING; 1173111.SAMN05444955_102148; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000199695; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.40; -; 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; 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:SF3; NEUTRAL PROTEASE B; 1.
DR   Pfam; PF07504; FTP; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU366073};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199695};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           29..535
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023155442"
FT   DOMAIN          81..130
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          145..218
FT                   /note="PepSY"
FT                   /evidence="ECO:0000259|Pfam:PF03413"
FT   DOMAIN          226..370
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          373..534
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        450
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   535 AA;  59164 MW;  5D4EA596B3347F61 CRC64;
     MKKRAAVGMV LSIALGASSF LFQQPAEAKG GEEIRYSKEY KTPAYIGEKW SKPKNLKNEE
     IVWAYLHAKK SLFKLKGDVK SQFKILKQEK DSLGMTHYRV QEVYHGIPVY GSDQTVHTDR
     DGNVTSFFGT VIPDLGAKKI QTTAKIGKEQ AVQIVRKDLE AQPGNISRLA SDPDTGLYIY
     PHQGNYYLAY HVKVSVIQPE PGYWHYFINA VNGEVIRKYN TVHQLTGSGR GVLGDRKTFE
     VDHKYGKYYL KGTSRGGGIK TYNAYHVIYE SQLPGTMVSS KTNYFLDGAA VDAHAYAEKV
     YDYFKNVHGR NSYDGNGAPV ISSVHVGRNW NNAAWIGTQM VYGDGDGIVF RPLSGALDVV
     GHELTHAITE KTANLEYHNE SGALNESISD IFGAMVDSGD WLLGEDVYTP KQSGDAFRSM
     SNPTQYDQPD HYSRYVRLPD TPDGDYGGVH INSGINNKAA YLLAEGGTHY GVNVTGIGRA
     KTAKIYYRAL TLYLTSRSTF ADMRQAAIKA ATDLYGSASQ EVQSVKNAYS AVGVY
//
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