(data stored in SCRATCH zone)

HOGENOM: ECOUM_1_PE1008

ID   ECOUM_1_PE1008                       STANDARD;      PRT;   274 AA.
AC   ECOUM_1_PE1008; E1RT33;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Penicillin-insensitive murein endopeptidase; EC=3.4.24
DE   -;AltName: Full=D-alanyl-D-alanine-endopeptidase; (ECOUM_1.PE1008).
GN   Name=mepA; OrderedLocusNames=UM146_05170;
OS   ESCHERICHIA COLI UM146.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=869729;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOUM_1.PE1008.
CC       Escherichia coli (strain UM146) chromosome, complete sequence.
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E1RT33_ECOUM
CC   -!- FUNCTION: Involved in the removal of murein from the sacculus. May
CC       also facilitate integration of nascent murein strands into the
CC       sacculus by cleaving the peptide bonds between neighboring strands
CC       in mature murein (By similarity).
CC   -!- CATALYTIC ACTIVITY: Splits the D-alanyl-gamma-meso-2,6-diamino-
CC       pimelyl peptide bond connecting neighboring peptidoglycan strands.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit. Zinc ion 1 is bound in
CC       the active site. Zinc ion 2 is bound at the dimer interface by
CC       residues from both subunits (By similarity).
CC   -!- SUBUNIT: Dimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M74 family.
CC   -!- GENE_FAMILY: HOG000276210 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E1RT33; -.
DR   EMBL; CP002167; ADN70439.1; -; Genomic_DNA.
DR   ProteinModelPortal; E1RT33; -.
DR   SMR; E1RT33; 20-274.
DR   GenomeReviews; CP002167_GR; UM146_05170.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:HAMAP.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   HAMAP; MF_01623; MepA; 1; -.
DR   InterPro; IPR009045; Hedgehog/DD-peptidase.
DR   InterPro; IPR005073; Peptidase_M74.
DR   Gene3D; G3DSA:3.30.1380.10; Hedgehog/DD-pept_Zn-bd; 1.
DR   Pfam; PF03411; Peptidase_M74; 1.
DR   PIRSF; PIRSF018455; MepA; 1.
DR   SUPFAM; SSF55166; Hedgehog_sig_N; 1.
DR   HOGENOMDNA; ECOUM_1.PE1008; -.
KW   ADN70439.1000068575old_1320000031;
KW   Complete proteome; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Periplasm; Protease; Signal; Zinc.
SQ   SEQUENCE   274 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNKTAIALLA LLASSASLAA TPWQKITQPV PGSAQSIGSF SNGCIVGADT LPIQSEHYQV
     MRTDQRRYFG HPDLVMFIQR LSRQVSNLGM GTVLIGDMGM PAGGRFNGGH ASHQTGLDVD
     IFLQLPKTRW TSAQLLRPQA LDLVSRDGKH VVPALWKPEI FSLIKLAAQD KDVTRIFVNP
     AIKQQLCLDA GTDRDWLRKV RPWFQHRAHM HVRLRCPADS LECEDQPLPP PGDGCGAELQ
     SWFEPPKPGT TKPEKKTPPP LPPSCQALLD EHVI
//

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