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Database: UniProt
Entry: A8G005_SHESH
LinkDB: A8G005_SHESH
Original site: A8G005_SHESH 
ID   A8G005_SHESH            Unreviewed;       469 AA.
AC   A8G005;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:ABV38428.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Ssed_3824 {ECO:0000313|EMBL:ABV38428.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV38428.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV38428.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV38428.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; CP000821; ABV38428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8G005; -.
DR   STRING; 425104.Ssed_3824; -.
DR   KEGG; sse:Ssed_3824; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_1_1_6; -.
DR   OMA; PGDSYAQ; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          57..193
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          202..376
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   469 AA;  52603 MW;  F4B34E33878821F1 CRC64;
     MLVTSLTTAA LFVPVVTANE LNLQQMAAPL YRTEKQIIFH RLDNGLQLRL LPLADNQLVS
     LASQFNVGSR DEPSGQTGYA HLFEHMLFKG SENAPGDSYA QTMSAISGQF NASTFFDFTN
     YYLTIPSEAL KLSLWLEADR FIRPALTDQT VKNQQDTVLE EMATSIDNQP YVRKAMEFLL
     TQARDTPYGH AVIGSREDVK NATKEALKQF HHNHYRPDAM QLSIVGALPE NTTLWVEEEF
     GQWQNPEQAL KPPLKMQFEN KLVHAEVIDE RGPWPALLLA WHTVGQTHSD AAAVSLLEAY
     LFQNRSSLIK QSGLTEPDQL LTYSIPMTME QMGVSNLIMV PRAKTSLDQL AGNVEQAIET
     LATDGISDED LSQLKANWLN KRLQLIDRPS LLARALSATL AQDSLTPLTG PWERINAVSP
     AMLQAAAQTY FSQGYVRLNL LPPWYIRWTK TLLEWFPTGV SDTLEDLVL
//
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