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Database: UniProt
Entry: R8AUD1_PLESH
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Original site: R8AUD1_PLESH 
ID   R8AUD1_PLESH            Unreviewed;      1017 AA.
AC   R8AUD1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Peptidase M66, StcE {ECO:0000313|EMBL:EON89920.1};
GN   ORFNames=PLESHI_03139 {ECO:0000313|EMBL:EON89920.1};
OS   Plesiomonas shigelloides 302-73.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Plesiomonas.
OX   NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON89920.1, ECO:0000313|Proteomes:UP000014012};
RN   [1] {ECO:0000313|EMBL:EON89920.1, ECO:0000313|Proteomes:UP000014012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=302-73 {ECO:0000313|EMBL:EON89920.1,
RC   ECO:0000313|Proteomes:UP000014012};
RX   PubMed=23814109;
RA   Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT   "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL   Genome Announc. 1:e00404-13(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01031};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01031};
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:EON89920.1}.
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DR   EMBL; AQQO01000023; EON89920.1; -; Genomic_DNA.
DR   AlphaFoldDB; R8AUD1; -.
DR   STRING; 703.SAMEA2665130_00797; -.
DR   MEROPS; M66.001; -.
DR   PATRIC; fig|1315976.3.peg.605; -.
DR   HOGENOM; CLU_009979_0_0_6; -.
DR   OrthoDB; 6229465at2; -.
DR   Proteomes; UP000014012; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   CDD; cd12214; ChiA1_BD; 1.
DR   CDD; cd12215; ChiC_BD; 1.
DR   Gene3D; 2.60.120.1230; -; 2.
DR   Gene3D; 2.60.40.2550; -; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR019503; Peptidase_M66_dom.
DR   InterPro; IPR048990; StcE_b-sandwich.
DR   InterPro; IPR022218; TagA_dom.
DR   PANTHER; PTHR39540; -; 1.
DR   PANTHER; PTHR39540:SF1; DICTOMALLEIN-1-RELATED; 1.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF10462; Peptidase_M66; 1.
DR   Pfam; PF20944; StcE_b-sandwich; 2.
DR   Pfam; PF12561; TagA; 1.
DR   SMART; SM00495; ChtBD3; 2.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51694; PEPTIDASE_M66; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01031};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01031};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW   ProRule:PRU01031};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01031}; Reference proteome {ECO:0000313|Proteomes:UP000014012};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01031}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1017
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004462255"
FT   DOMAIN          283..538
FT                   /note="Peptidase M66"
FT                   /evidence="ECO:0000259|PROSITE:PS51694"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT   BINDING         433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT   BINDING         437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT   BINDING         443
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
SQ   SEQUENCE   1017 AA;  110672 MW;  F4C3178584AA0B54 CRC64;
     MEMSYLSCLI AASLVTAALP VSANDTSPLY FNSIQPKNDL VGKLEAKVQF AQSQILPFKA
     LEGDRQPILT SLRKSLILVQ PLQPDAVTPM FVDARDSSGA LLGTVTLAPP SALPETVYHL
     PGVPAGGVNF TPESGETRVI NSSAELAKLD DKNGTFLKER LATSALVEIQ TADGRWVRDI
     YLPQGAELEG KMVRISSRAG YNSNLYYGER KVTVSNGQTI AFKYANGQWF REGELANNRL
     SYAPDTWSGE LPAEWIVPGL TLSVRQGNLT GELTDIPVGA PGELLLHTID IGMLVEPRDR
     FLFAKDFDAQ REYFQTLPAR RMVVNQYAPL YLPEVMLPNG TLLTDFDPSD GGWHGGTMRQ
     RIGKELISHG IDNANYGINS SAGEGEGSHP FVVAQLAAHN SRGKYANGVQ VHGGSGGGGI
     VTLDNSLGNE FSHEVGHNFG LGHYVDGFRG SVHRSADQIN STWGWDSDKL RFIPNFFPRQ
     NQAETCLDGQ CQLPFDGRQF GKDAMAGGEP FSAANRFTLY TPNSAALIQR FFASKAVFDS
     QSPTGFSKWN ADTARMEPYQ HTVEGLETVN APVDNLSAEN LAQLLSEYEL VKIGMWNGHW
     ARNIYMPAAS SENRGRSISI DHRAGYNSHL FINGSEILVS NGYKKTFTSD GQRWQERAEV
     NTRVARQPQH FEIPVTTLVG YYDPQARLQS YIYPALHAAY GFTYPDDSAT VSSNDCQLQV
     ETRDSVLRFK LLNHRASSAV MNKFHINVPS DSQPSKARVV CNNRTLSETP LSAAPTDLVY
     TINGKLPETE GGGECSNAWR AEATYVGGDL ASHNGKSWRA EWWTQGEEPG TTGEWGVWRQ
     QGDSDCSGGV TPPPVTGSSD FTLSNLDSRY ALVNGQVSIR LNLTTQNPVQ IAASLQQNGQ
     RFGEVSAQVN GNSALTLAVS NASAGSYELV IEGKAEGQQP VVQRHPVTLS EDNQGGGSEG
     DYPAYVAGNS YQAGDRVSNS GANYECKPWP YSGWCGLSPA HYAPGTGSAW SDAWQRL
//
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