ID A0A1E4HET9_9GAMM Unreviewed; 530 AA.
AC A0A1E4HET9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=ABS82_08265 {ECO:0000313|EMBL:ODT95425.1};
OS Rhodanobacter sp. SCN 67-45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1660133 {ECO:0000313|EMBL:ODT95425.1, ECO:0000313|Proteomes:UP000094158};
RN [1] {ECO:0000313|EMBL:ODT95425.1, ECO:0000313|Proteomes:UP000094158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODT95425.1}.
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DR EMBL; MEFB01000044; ODT95425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4HET9; -.
DR Proteomes; UP000094158; 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; 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:SF1; BACILLOLYSIN; 1.
DR Pfam; PF07504; FTP; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 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};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 25..530
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023030246"
FT DOMAIN 71..102
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 230..371
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 374..525
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 364
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 453
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 530 AA; 56186 MW; 7690432B7FBC7E2B CRC64;
MLNKKLVAAL VLALGGATAA SCMAATPLHI HAGAMGRIAP ATLANRLGLG ADASFQADRQ
LRTAHGTLKS RERQTWRGVP VYGRSVVVER DTRGAVLSVA GSAERDIGAQ LASAQPRLTA
AAATAALRRH MGDTGLAARN VDSELFVYPQ AGRAPRLTYR VSYVLDNHGQ PSRPTAIVDA
DTGAVLKQWD GLAHGRRPPG GGSTPVAVTA TGPGGNALTG SYNYDNSGPG RERLDAVRIG
SVCYLQDADV ATYNLAGGQR VTQWSFGCAG SNPALWVSQG DAINGAYSPI NDAHHFGGVV
HDMYSTWFGE PPLKNTDGSA MQLSMWVHYG TNYENAFWDG REMVFGDGDQ YFFPFVVLDV
TGHEISHGFT EQHSGLEYTG QSGGMNEAFS DMAGEAVKYF DRGSNDFMVG ADMVKPATVP
LLGMAALRDM CTPSNDGASI DSARDYNDSL DVHYSSGVYN RAFCLLAKTS GWNTRKAFEV
FHDANALYWS PQETFDGGAC GVEQAATDRG YAEADVAAAF NAVDVACAAP
//
