ID A0A2S1JUH5_9GAMM Unreviewed; 938 AA.
AC A0A2S1JUH5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:AWF82059.1};
GN ORFNames=BTJ40_15165 {ECO:0000313|EMBL:AWF82059.1};
OS Microbulbifer sp. A4B17.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=359370 {ECO:0000313|EMBL:AWF82059.1, ECO:0000313|Proteomes:UP000244764};
RN [1] {ECO:0000313|EMBL:AWF82059.1, ECO:0000313|Proteomes:UP000244764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4B17 {ECO:0000313|EMBL:AWF82059.1,
RC ECO:0000313|Proteomes:UP000244764};
RX PubMed=16885309; DOI=10.1128/AEM.00494-06;
RA Peng X., Adachi K., Chen C., Kasai H., Kanoh K., Shizuri Y., Misawa N.;
RT "Discovery of a marine bacterium producing 4-hydroxybenzoate and its alkyl
RT esters, parabens.";
RL Appl. Environ. Microbiol. 72:5556-5561(2006).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP029064; AWF82059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1JUH5; -.
DR KEGG; mii:BTJ40_15165; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000244764; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 72..194
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 228..403
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 514..638
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 668..847
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 938 AA; 104042 MW; E405369D194FE329 CRC64;
MDLRPLLISV AIAITGLTAC GKSTDDTPHA LSVDREAAAS SKAAASDQGA YVPPPKLEIP
FHKEVLPNGL TVIVHEDHKA PVVSTNIWYK VGSKDEPEGK TGFAHLFEHL MFNGSENFPG
EYFEPFQRSG ATDMNGTTSN DRTNYFVTVP KGALDMALWM ESDRMGHFKG AITQEVLDEQ
RGVVKNEKRQ GENAPYGKAF DIIAKSTFPK GHPYSWTPIG SMEDLDNASL EDVKKWFEDH
YQPANAILVI AGDVTVKDAM AKARKYFADI PSTGVQPRIK NWELPTQVKK REVVYDQVPQ
TRIYKVWNVP AVGSEVEDAL ELMTSLLANR KNSLLYRRLV RDEQVATSVS AFYYGRQLAG
QLMIIVDVKP GQSVEKVENL LNEELKQFAT NGVSAEELRR VKQSEFAGLV KGLEKTGGFG
GKSDILAQSE FYFGDPGALI EGIEDYANVS ALEVQEVAQQ WLKEDSYTLI MEPKQKFTAA
TEGADRSKLP EVDKNVELEL PKQKEFTLKN GLKVVLAERH DTPVVLMNLQ FRSGASTDKN
KPGLASVAAQ MLNEGAGNLD SLEFSSRAEE LGVSIGGGSS LDYNNISMSA LKTQLEPSLE
LFEKVVTEPR FPESDLERVK SNRLDAIAQE KAQPQGLAMR ELPPLLFGEN HPYGSPLTGS
GTPEGIKSIT REDLVNFQKT WVRPDNATLT IVGDVTEKEI EPLLNETLGK WTAPKAELPK
IEVAKVPRPE KARVYLLDRP GAQQSYIMAG LLMPPWQPQG AEAFDAMANI IAGKFTSRVN
MNLRENKHWS YGARAVSLDT EGQRPYILFA PVQTDKTAPA IKELVKEYED YLGDRPITEK
ELEDYQNDEV LKQSARFQTK GQLLSSINWQ VEKGLPEEYI AEYPQRVSAL NKEKVEASAK
EYLAPEQFTW VIVGDLSKIK GEVEALDIGP VEVLPTKD
//
