ID A0A094K2L4_9GAMM Unreviewed; 916 AA.
AC A0A094K2L4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KFZ38896.1};
GN ORFNames=HR45_00370 {ECO:0000313|EMBL:KFZ38896.1};
OS Shewanella mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1515746 {ECO:0000313|EMBL:KFZ38896.1, ECO:0000313|Proteomes:UP000029264};
RN [1] {ECO:0000313|EMBL:KFZ38896.1, ECO:0000313|Proteomes:UP000029264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YQH10 {ECO:0000313|EMBL:KFZ38896.1,
RC ECO:0000313|Proteomes:UP000029264};
RA Liu Y., Zeng R.;
RT "Shewanella sp. YQH10.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:KFZ38896.1}.
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DR EMBL; JPEO01000001; KFZ38896.1; -; Genomic_DNA.
DR RefSeq; WP_037438589.1; NZ_JPEO01000001.1.
DR AlphaFoldDB; A0A094K2L4; -.
DR STRING; 1515746.HR45_00370; -.
DR eggNOG; COG0612; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000029264; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
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:UP000029264};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..916
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001906369"
FT DOMAIN 56..175
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 208..380
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 498..616
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 643..821
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 916 AA; 100839 MW; 77784474D2F807A9 CRC64;
MKNFNKTVVS ALLSGMLWLP SAVVPASEIP QHALAKINIE YQTFTLPNGL TTIVHTDHSV
PNIYVGVWYK VGSKNEPEGK TGFAHLFEHL MFQETIHRDG EYFLPFDKAG AVGMNGTTSQ
DRTNYYETVP SNAIDLALWM ESDRMGYLGP SITQALLDEQ RAVVQNEKRQ GQLRPGAKIY
ERFLANFYPK GHPYDHTTIG SMKDLNNASL DDVKQWFKDA YGATNAVLVL SGDIDLATAK
EKVAHYFSDV PAGKPMDKID QWIPTLKHIK RDIIYDKVAN VSLSRVWPLP NGSDKDTTLM
ELVSRTLAGG KNTPLYDVLV DEKQLAVSVS ANVSANDVNS TFSLDVTLKP NANAEEVERI
IDQTLQKFFK QGPEEEQLAA INLGGEISLL RSMESNEAIG SQLIRGMVHH DDPLFVNKKR
QWISSADSDD VRKVAKKWLD KPYYEARLLP EPSTQPMQAQ VDRSKLPQVG EFNGKITMPP
IHQAVLDNGM KLVVAERHNL PLVDVSMQFT TGSLADKFYA PGTASQAFGM LTMGSDKYDM
GELAKKMDSI GVGINGSAGS QGSGVSWSSL SSNMDDAFAL AAEVIRHPTY PQSELNKLID
NLDSSYDNYE LEPLRSATDV YGKAIWGGQH PFGHIVTREE AKKVNRATIE KFHDSEIGPN
NATLYLVGDV TLAQATKLAN KYFGSWHQVK PTPLPAITAP QGDVGKVILV DAPGAVQSSI
SVGHAVAPFD KDKAATQMLM DAALGQGFNS RLNMNLREQK GWAYGFGANI SNVPVGDRVF
TASGTVQTDK TAAAMSEIKR EIREYVSTKP QTEAELERDK AATVHSIPQG FTNNGAFMKT
MINADLYHLP YTRIEGAAER LSKVILAQTR ALAQATYKPD ALTWVIVGDL SKIEKDVRAL
KLGPVEVWDV YGNKLR
//