ID A0A0Q9JB78_9MICO Unreviewed; 371 AA.
AC A0A0Q9JB78;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=ASG80_05425 {ECO:0000313|EMBL:KRE26391.1};
OS Agromyces sp. Soil535.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1736390 {ECO:0000313|EMBL:KRE26391.1, ECO:0000313|Proteomes:UP000051793};
RN [1] {ECO:0000313|Proteomes:UP000051793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil535 {ECO:0000313|Proteomes:UP000051793};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE26391.1, ECO:0000313|Proteomes:UP000051793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil535 {ECO:0000313|EMBL:KRE26391.1,
RC ECO:0000313|Proteomes:UP000051793};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KRE26391.1}.
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DR EMBL; LMRW01000012; KRE26391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9JB78; -.
DR STRING; 1736390.ASG80_05425; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000051793; 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; 1.10.390.10; Neutral Protease Domain 2; 1.
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; 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 Secreted {ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 112..193
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 196..365
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT REGION 56..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 287
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 371 AA; 40295 MW; BEA45B526E2D98E5 CRC64;
MPRPYPHPSP HAAIVPPYLL ARIATADDPR FDAAADAARR SLLRDAPMRE WRAAGELPSF
IAPEHPARDE RPAAAPGTAP QPDRRISDAE HDDKLPGRLV RREGQPPSGD LAVDQAYVGL
GDTFELFARV FARDSIDGAG MPLEATVHYG DRYDNAFWDG ERMVFGDGDG EVFSGFAGSL
SVIGHELAHG VTERTARLRY QGQSGALNEH VSDVFGALVE QYSMGQDAAS ATWLIGEGVF
TDAVEGRAIR SMKEPGTAYD DDLLGKDPQP DHFDRYIETD EDNGGVHLNS GIPNRAFALA
ALELGGFAWE TVGRVWYDVL TSGRLRPDTD FHTFAAETVR AARERYGRTS REARAVAGGW
AAVGIEVPPT S
//
