ID A0A1F3NKM5_9BACT Unreviewed; 360 AA.
AC A0A1F3NKM5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=A2Y71_00445 {ECO:0000313|EMBL:OFY64785.1};
OS Bacteroidetes bacterium RBG_13_42_15.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797355 {ECO:0000313|EMBL:OFY64785.1, ECO:0000313|Proteomes:UP000178321};
RN [1] {ECO:0000313|EMBL:OFY64785.1, ECO:0000313|Proteomes:UP000178321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFY64785.1}.
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DR EMBL; MEOS01000190; OFY64785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3NKM5; -.
DR Proteomes; UP000178321; 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 96..181
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 184..352
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 174
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 275
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 360 AA; 40232 MW; 5370CF5212661E4B CRC64;
MIAPCNCILC ITPPYMLEKI LKHGTQKQKR RALKALTMSA QFRGRRQALI NITFPVRRTP
QPVKHRLVYH AGFKEIIRGR LVRKEGEGPS GDPAIDEAYD GAGHTWDLYY DVFGRNSVDN
KGMHLLSTVH YGQGYDNAFW DGEQMVYGDG DEDLPEPERL FRRFTIAVDI IGHELTHGIT
QFEAKLAYYG QSGALNESFS DVFGSLVKQR ILNHTASEAD WLIGQDIFTS NVNGQAIRSM
KSPGTAYDDP LLGKDPQPGH MKDYVNTVSD NGGVHFNSGI PNRAFYICAN EIGGYAWKKA
GRIWYKALRD RLKADTDFQE AADITFRIAG EEYGTGSKEQ NAVKKGWAEV GISTGTDKKS
//
