ID E5B7J4_ERWAM Unreviewed; 338 AA.
AC E5B7J4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN Name=prt1 {ECO:0000313|EMBL:CBX81449.1};
GN ORFNames=EAIL5_2629 {ECO:0000313|EMBL:CBX81449.1};
OS Erwinia amylovora ATCC BAA-2158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX81449.1};
RN [1] {ECO:0000313|EMBL:CBX81449.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX81449.1};
RA Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E.,
RA Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.;
RT "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity
RT Restricted to Rubus Plants.";
RL J. Bacteriol. 193:785-786(2011).
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; FR719194; CBX81449.1; -; Genomic_DNA.
DR AlphaFoldDB; E5B7J4; -.
DR MEROPS; M04.027; -.
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 InterPro; IPR032475; Protealysin_N_PP.
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 Pfam; PF16485; PLN_propep; 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:CBX81449.1};
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 4..40
FT /note="Protealysin N-terminal propeptide"
FT /evidence="ECO:0000259|Pfam:PF16485"
FT DOMAIN 58..166
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 169..336
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 260
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 338 AA; 37492 MW; 58EDD91CAE830247 CRC64;
MPYGVIPPYI LSKIINNGSS HQQRCARQTL THVQTLMNES WQAPHSAITA TPGNVQREIY
DAQQTQNLPG QRVRSGDLPA SNDAAVDEAW DYLGITYDFF WHAYQRNSLD NEGLTLLGTV
HYGRDYQNAF WNGQQMVFGD GDGEIFNRFT IALDVVGHEL AHGVTETEAG LIYFEQAGAL
NESLSDVFGV LVKQYHLQQS AEQANWLIGE GLLAEGINGR GLRSMSEPGS AYDDPLLGKD
PQPAHMRDYL RTREDNGGVH LNSGIANRAF YLAAVALGGY AWEMAGYAWY DTVCDKELPQ
IADFKTFAEF TVHHGEKRFN KATGAAIKDA WKQVGVLT
//
