ID   C1A9T1_GEMAT            Unreviewed;       470 AA.
AC   C1A9T1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Putative M16B family peptidase {ECO:0000313|EMBL:BAH39258.1};
GN   OrderedLocusNames=GAU_2216 {ECO:0000313|EMBL:BAH39258.1};
OS   Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS   100505).
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH39258.1, ECO:0000313|Proteomes:UP000002209};
RN   [1] {ECO:0000313|Proteomes:UP000002209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC   {ECO:0000313|Proteomes:UP000002209};
RA   Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA   Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA   Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT   "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT   novel phylum Gemmatimonadetes.";
RL   Submitted (MAR-2006) 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; AP009153; BAH39258.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1A9T1; -.
DR   STRING; 379066.GAU_2216; -.
DR   KEGG; gau:GAU_2216; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_1_1_0; -.
DR   Proteomes; UP000002209; 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; 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:SF35; NON-CATALYTIC MEMBER OF PEPTIDASE SUBFAMILY M16B-RELATED; 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:UP000002209};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..470
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002906755"
FT   DOMAIN          72..173
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          213..388
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   470 AA;  51703 MW;  6A25631C43245970 CRC64;
     MNVSHAPRPR GALVRATLGS LAAAAALLAT ASLSAQSAPS IPHEKYSLPN GLEVILHVDR
     SVPIIAVEGF YKVGSGDEKK GRTGFAHLFE HVMFMGSQNV PVGKFDEWLE AAGASNNGST
     NFDRTNYYET GPSNALPLML WLDADRMGWL LPTMDQEKLD LQRGVVQNER RQSYDNVPYG
     RAFETILPVM FPSNHPYSWP VIGSMADLSA AALDDVKDFF RQYYAPNNAT ITIAGDFNAD
     SVKAQVTKYF GSIPRSAQPV VRPTVPEVRI AKDTVLVMED RVQLPRAYYA WHGVKAFSPD
     DAALDALTDI IAGGKSSRLY RTLVYEKQIA QDVSMGNTSQ KLDGLIMLTA TAKPGVHPRE
     MDVEIRKTLN DIATSGVTDR ELTRVKNGMR ASMLDRLSSV LGKATQLSYY NYYTGTPDYM
     AQDLARYERL TSADLQRVAR QYVLQPKIVL TVVPEGKKEL ALTSAQGGNN
//