ID Q0RGY3_FRAAA Unreviewed; 368 AA.
AC Q0RGY3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN OrderedLocusNames=FRAAL4610 {ECO:0000313|EMBL:CAJ63252.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ63252.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ63252.1, ECO:0000313|Proteomes:UP000000657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CT573213; CAJ63252.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0RGY3; -.
DR STRING; 326424.FRAAL4610; -.
DR MEROPS; M04.027; -.
DR KEGG; fal:FRAAL4610; -.
DR eggNOG; COG3227; Bacteria.
DR HOGENOM; CLU_008590_0_1_11; -.
DR Proteomes; UP000000657; Chromosome.
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 ECO:0000313|EMBL:CAJ63252.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 97..196
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 199..366
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 290
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 368 AA; 39688 MW; F09DA724B0CFA9EF CRC64;
MPCPRPTATS PVSPGATVPG PTVPCAVPPH VLERIVRNGS DDQRSWALST LLQDSSHRTI
RLHNAQLRSA QRGVVPPRLD PDAGPRRTVA DAAGTESLPG RTVRTENEPA VDDVAVNEAY
DGLGATFRFY SEVFGRDSID DEGVGLLASV HYGDHYDNAF WNGRQMVFGD GDGELFQRFT
VSLDIIGHEL THGVTEDEAA LMYVNQSGAL NESVSDVFGS LVKQYALGQT AEQADWLIGD
ELLTDAVQGV ALRSLKDPGT AYDDPVLGDD IQPAHMTGYV QMTGDNGGVH INSGIPNKAF
YLAAIALGGY AWERAGRIWY ESLRAPQVRP NATFRSFAAA TRRQAGVLFG ADERKAVTEA
WREVGIAV
//
