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
//