ID   B9L9P8_NAUPA            Unreviewed;       408 AA.
AC   B9L9P8;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Peptidase, M16 family {ECO:0000313|EMBL:ACM92750.1};
GN   OrderedLocusNames=NAMH_0954 {ECO:0000313|EMBL:ACM92750.1};
OS   Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC   Nautiliaceae; Nautilia.
OX   NCBI_TaxID=598659 {ECO:0000313|EMBL:ACM92750.1, ECO:0000313|Proteomes:UP000000448};
RN   [1] {ECO:0000313|EMBL:ACM92750.1, ECO:0000313|Proteomes:UP000000448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1463 / DSM 18972 / AmH
RC   {ECO:0000313|Proteomes:UP000000448};
RX   PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA   Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA   Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT   "Adaptations to submarine hydrothermal environments exemplified by the
RT   genome of Nautilia profundicola.";
RL   PLoS Genet. 5:E1000362-E1000362(2009).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CP001279; ACM92750.1; -; Genomic_DNA.
DR   RefSeq; WP_015901802.1; NC_012115.1.
DR   AlphaFoldDB; B9L9P8; -.
DR   STRING; 598659.NAMH_0954; -.
DR   KEGG; nam:NAMH_0954; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_1_0_7; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000000448; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001431; Pept_M16_Zn_BS.
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.
DR   PROSITE; PS00143; INSULINASE; 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          24..131
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          171..344
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   408 AA;  47220 MW;  0DE100EACB9BE74F CRC64;
     MLHKFYKQKL KNNLEVIVVP MNKGSNVITS NIYYKVGSRN EIMGKSGIAH MLEHMNFKST
     KNLAEGEFDK IIKSLGGVDN ASTGFDYTHY YIKTSSAYLD KTFELFSEVM ENLNLNDDEF
     QRERKVVYEE RLWRTDNNPI GYLYFRLFNN TYLYHPYHWT PIGFKDDILN WSIEDIRSFH
     KTFYQPKNAF LLVAGDIDPE DVFNLADKYF SHIKNSRKIP KVHMKEPELD GDRHVVIQRD
     TEVDIVAIAY RIPDFKHEDQ FALSAYSEIL SGGKSGVLRE KLINKKRLVS EVYAYNMELI
     DPGVFLALAI CNPGVSPDLV ENELKKTLLN TKITKKALNK VKNQTKMDFL TQLESSSGVS
     NVYGDYFAKG DITPLLEYED KINALTPEKV EDIKKYFDKS VTVKLIKK
//