ID A0A0S9CNM7_9MICC Unreviewed; 356 AA.
AC A0A0S9CNM7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=ASE96_03675 {ECO:0000313|EMBL:KQN95283.1};
OS Arthrobacter sp. Leaf69.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN95283.1, ECO:0000313|Proteomes:UP000051467};
RN [1] {ECO:0000313|EMBL:KQN95283.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN95283.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN95283.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN95283.1,
RC ECO:0000313|Proteomes:UP000051467};
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:KQN95283.1}.
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DR EMBL; LMLR01000001; KQN95283.1; -; Genomic_DNA.
DR RefSeq; WP_056426054.1; NZ_LMLR01000001.1.
DR AlphaFoldDB; A0A0S9CNM7; -.
DR STRING; 1736232.ASE96_03675; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000051467; 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 90..173
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 176..345
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT REGION 35..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 267
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 356 AA; 37991 MW; 0A16CCE603E36602 CRC64;
MHCSIIPPYM LRRLAAQRVP ELSDAARAAK EALHHVPSFQ ASRAMPGPGS HPGLREPKPA
APERTVYDAK FTDQLPGSAV RKEGEPPTGD PAADEAYDGL GHTHRLYAEA FGRNSIDGNG
LHLDATVHYG RLYDNAFWDG QQMVFGDGDG QVFQRFTKSL SVIGHELAHG VTQYSAGLVY
RNQAGALNES MSDVFGALVE QFVQQQPAAA AGWLIGEGLF TDQVQGTALR SMKAPGTAYD
DDVLGKDPQP DSMDGYVHTS ADNGGVHINS GIPNRAFYLV ATTLGGNAWD APGRIWYETL
TGGTLSPTAT FGAFAKATAA SAKELFGADS AEHDAVRSAW ETVKVKLPGA RRKPSS
//
