ID   A0A1H2MZ24_9ACTN        Unreviewed;       497 AA.
AC   A0A1H2MZ24;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=SAMN04488544_3007 {ECO:0000313|EMBL:SDU98509.1};
OS   Microlunatus sagamiharensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Microlunatus.
OX   NCBI_TaxID=546874 {ECO:0000313|EMBL:SDU98509.1, ECO:0000313|Proteomes:UP000198825};
RN   [1] {ECO:0000313|Proteomes:UP000198825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21743 {ECO:0000313|Proteomes:UP000198825};
RA   Varghese N., Submissions S.;
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|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; LT629799; SDU98509.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2MZ24; -.
DR   STRING; 546874.SAMN04488544_3007; -.
DR   Proteomes; UP000198825; Chromosome i.
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; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR049457; Emfourin.
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; PTHR43579; -; 1.
DR   PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 1.
DR   Pfam; PF20242; Emfourin; 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|RuleBase:RU366073};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198825};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   DOMAIN          81..182
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          185..353
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          55..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        276
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   497 AA;  52531 MW;  420BB14634FF58F5 CRC64;
     MTPTADADRR SPQAIRCSFV PPYLLRRLAE SDPGRRLLAD GRDTLAVDER MRSRREAATA
     TTAPAVPDTG GNRVVYDAGG AEELPGRRAR DEDDPATGDA AVDEAHAHSG VSWDLFAEVF
     DRPSVDGRGT PLTVTVHYGR DYDNAFWDGE QLVFGDGDGE VFDRFTKPLD VTAHEFTHGV
     TQFSAGLTYQ GQSGALNESV SDVFASLAKQ RSLGQDASQA DWLIGQGLFM PDVKATALRS
     MLEPGTAYDD PRLGRDPQVG SMDDYVDTEE DNGGVHLNSG IPNRAFALAA RAIGGPSWEK
     AGQVWYAALT GGAVTPSTDF EGFAAATVDA AARLYPEDTS VADHVREAWQ QVGLARGTQA
     VAAQTPPSGG PAPAGPGGGS PSAKPQAPAG APDPVGSAGV PSLPGQPGDD VVAVRRSGGF
     TGASQFAQLS LTDDPAGTEL RRLLDQISVS DLGRSEPQPD RFTYTVACRS FELTVPEQDL
     TPELTRVVQI VLDQRAR
//