ID   A0A1I3EBT8_9RHOB        Unreviewed;       447 AA.
AC   A0A1I3EBT8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:SFH96450.1};
GN   ORFNames=SAMN05216258_103287 {ECO:0000313|EMBL:SFH96450.1};
OS   Albimonas pacifica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Albimonas.
OX   NCBI_TaxID=1114924 {ECO:0000313|EMBL:SFH96450.1, ECO:0000313|Proteomes:UP000199377};
RN   [1] {ECO:0000313|EMBL:SFH96450.1, ECO:0000313|Proteomes:UP000199377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.11030 {ECO:0000313|EMBL:SFH96450.1,
RC   ECO:0000313|Proteomes:UP000199377};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOQH01000003; SFH96450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3EBT8; -.
DR   STRING; 1114924.SAMN05216258_103287; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000199377; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase 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; 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   Hydrolase {ECO:0000313|EMBL:SFH96450.1};
KW   Protease {ECO:0000313|EMBL:SFH96450.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199377};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..447
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011716165"
FT   DOMAIN          41..185
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          192..366
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   447 AA;  48216 MW;  38BF269896590480 CRC64;
     MSRLARIVAP ALALLAVPFV PAQAATDVEI VTSPGGIVAW LVEEPSIPMV AIEISFEGGA
     SREPDDKVGV THFLSTMLDE GAGELESAAF SARADQLAMR YGFEAGRDSF TVSARMLSET
     RDASVELLRS ALVEPRFDPE PMERMRASIL ATLRDQATDP QAILARSWRE ELFGDDPYAR
     PMEGTPESVA AIDAGDLRAA RERALNRSRL AIGVVGDITA EELGPLLDRL LGDLPAEPWE
     PLGPAELSPD RDLTVIPFDI PQSSAAFVQE GLARDDPDFI PAYVMNHILG GGGFTSRLTE
     EVREKRGLTY GVYSYLAPYD RAALMAGGVA SANDRVAEAI EVIRAEWTRM RDEGVTEEEL
     EAAKRYLTGA YPLRFDSNAK IAGQLAGLME EGFTPAYLEE RNALIEAVTP ADIARVAARL
     LAPEALKVTV IGQPEGLPEA ERAAPAD
//