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Database: UniProt
Entry: A0A2T7G6E3_9RHOB
LinkDB: A0A2T7G6E3_9RHOB
Original site: A0A2T7G6E3_9RHOB 
ID   A0A2T7G6E3_9RHOB        Unreviewed;       436 AA.
AC   A0A2T7G6E3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:PVA09990.1};
GN   ORFNames=DC366_09985 {ECO:0000313|EMBL:PVA09990.1};
OS   Pelagivirga sediminicola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pelagivirga.
OX   NCBI_TaxID=2170575 {ECO:0000313|EMBL:PVA09990.1, ECO:0000313|Proteomes:UP000244446};
RN   [1] {ECO:0000313|EMBL:PVA09990.1, ECO:0000313|Proteomes:UP000244446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH-SD19 {ECO:0000313|EMBL:PVA09990.1,
RC   ECO:0000313|Proteomes:UP000244446};
RA   Ji X.;
RT   "Pelagivirga bohaiensis gen. nov., sp. nov., a bacterium isolated from the
RT   Bohai Sea.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:PVA09990.1}.
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DR   EMBL; QCYH01000005; PVA09990.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7G6E3; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000244446; Unassembled WGS sequence.
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; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000244446};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..436
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015713321"
FT   DOMAIN          38..175
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          188..362
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   436 AA;  47164 MW;  407ECD6B3A8BC6EA CRC64;
     MIRPLVLALA AALLAAPASA EIEVQDLTTP GGINLWLVED HTIPFVALEL RFRGGASLDL
     PGKRGATNLM TGLLEEGAGD MDSREFARRA EALAANFSYS VGDDMLAVSA RFLSENRDDA
     VALLRESLVN PAFNQKSIDR VRGQVNSIIE SDLKDPRAIA GRAFDSKTFG DHPYGTSKDG
     TLESVAGLTR DDIVAAHRAA LVRDRLYVSA VGDITADELT ELVDSLTQDL PQSSDIALPG
     DAKLDLVGDI TVIDFATPQS VVTFAQPGID RDHPDFFAAY LLNQILGGGG FESRLMNEVR
     EKRGLTYGVY SYLVDKDGAQ LWMGQVASAN DRVAQAIEVI KEEWQKMQQS GVTAQELEDA
     KNYMTGAYPL RFDGNAPIAN IAVEMQVEGL PTDYIATRND QVNAVTLEQI NRVARELLDP
     AKLSFVVAGQ PEGLPE
//
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