ID C9XY20_CROTZ Unreviewed; 341 AA.
AC C9XY20;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN Name=prt1 {ECO:0000313|EMBL:CBA32813.1};
GN OrderedLocusNames=Ctu_31020 {ECO:0000313|EMBL:CBA32813.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA32813.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(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; FN543093; CBA32813.1; -; Genomic_DNA.
DR AlphaFoldDB; C9XY20; -.
DR MEROPS; M04.023; -.
DR KEGG; ctu:CTU_31020; -.
DR PATRIC; fig|693216.3.peg.2933; -.
DR HOGENOM; CLU_008590_0_1_6; -.
DR Proteomes; UP000002069; 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 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:CBA32813.1};
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 9..45
FT /note="Protealysin N-terminal propeptide"
FT /evidence="ECO:0000259|Pfam:PF16485"
FT DOMAIN 62..170
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 173..340
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 163
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 341 AA; 37831 MW; 8165D42983A607E3 CRC64;
MNQSRYPTVI PPYILRRIID HGSEPQQQKA RQTLTHVQTL MAHHHAKAAV AHVSAKGELE
RDIYDAQNRE ELPGQIVRRE GEPSNGDVAV DEAYDYLGVT HEFFWKAYKR DSLDNKGLVL
SGTVHYGREY QNAFWNGQQM VFGDGDGEIF NRFTIAIDVV GHELSHGVTE TEAGLIYFEQ
AGALNESLSD VFGSLVKQYQ HQQTADQADW IIGEGLLAEG INGKGLRSMS EPGTAYDDPL
LGKDPQPGHM KDYVKTREDN GGVHINSGIP NRAFYLAATA IGGYAWEKAG YAWYDTVCDR
SLSQNADFAS FAKLTIEHGR KRSGDSVAQA IEQAWKTTGV L
//
