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Database: UniProt
Entry: A0A2N3IED7_9BACT
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Original site: A0A2N3IED7_9BACT 
ID   A0A2N3IED7_9BACT        Unreviewed;       547 AA.
AC   A0A2N3IED7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Peptidase family M1 {ECO:0000313|EMBL:PKQ68603.1};
GN   ORFNames=Rain11_1581 {ECO:0000313|EMBL:PKQ68603.1};
OS   Raineya orbicola.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Raineyaceae; Raineya.
OX   NCBI_TaxID=2016530 {ECO:0000313|EMBL:PKQ68603.1, ECO:0000313|Proteomes:UP000233387};
RN   [1] {ECO:0000313|EMBL:PKQ68603.1, ECO:0000313|Proteomes:UP000233387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPSPC-11 {ECO:0000313|EMBL:PKQ68603.1,
RC   ECO:0000313|Proteomes:UP000233387};
RA   Albuquerque L., Polonia A.R.M., Barroso C., Froufe H.J.C., Lage O.,
RA   Lobo-Da-Cunha A., Egas C., Da Costa M.S.;
RT   "Raineya orbicola gen. nov., sp. nov. a slightly thermophilic bacterium of
RT   the phylum Bacteroidetes and the description of Raineyaceae fam. nov.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634015-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
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:PKQ68603.1}.
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DR   EMBL; NKXO01000023; PKQ68603.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3IED7; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000233387; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd09603; M1_APN_like; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233387};
KW   Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT   DOMAIN          40..214
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          259..464
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        330
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        404
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ   SEQUENCE   547 AA;  63508 MW;  C7BAF0EC2BFE1406 CRC64;
     MNKFWLFVFF TFPLGIKAQF TRKDSLLGYL YPARACYDVK YYDLQLRINP EKKFISGQNT
     IIYTLTQDAQ EIQIDLAPEL QIKKILWGKK SVPFKREERA VRVRFSKRQR KGSTEKVTII
     YEGTPQEAKK APWDGGFVWQ KDKQSNPWIG VACQNVGASV WFPNKDHWSD KPDSVKLTYE
     VPSGLVAVAN GNLIKTETLS DGYARYVWKV SYPINNYNIT LNVAKYSHFT DTYTAQDGSK
     LALDYYVLPE NVEKAQKQFE QVKPMLACYE KLFDKYPFWN DGFALVETPY LGMEHQGAIA
     YGNKYLQGYL GGDLTSTGIG KLFDFIIIHE TGHEYWGNSV SADERAEMWI HEAFCTYTEA
     LYVECMWGKA KAFEYANGWK KIIQNDVPIV PPRHVNQEGS SDMYFKGALM IHTLRNIINS
     DDKWFAYLKE FYQTFKGKNT NTDEVVAFWN KKTGLELRPF FTQYLKFLQI PTFEYKIEGG
     KFQYRFKADV KDFRMPIVVK FGSTEMILNA STEWETIIFD ARGGNNSLLN EPFSVRTDLF
     FVNVERK
//
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