ID   D7N8U7_9FIRM            Unreviewed;       465 AA.
AC   D7N8U7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF0629_01370 {ECO:0000313|EMBL:EFI41312.1};
OS   Peptoniphilus sp. oral taxon 386 str. F0131.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=575609 {ECO:0000313|EMBL:EFI41312.1, ECO:0000313|Proteomes:UP000004712};
RN   [1] {ECO:0000313|EMBL:EFI41312.1, ECO:0000313|Proteomes:UP000004712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0131 {ECO:0000313|EMBL:EFI41312.1,
RC   ECO:0000313|Proteomes:UP000004712};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Peptoniphilus sp. oral taxon 386 strain F0131.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; GL349423; EFI41312.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7N8U7; -.
DR   STRING; 575609.HMPREF0629_01370; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_590123_0_0_9; -.
DR   Proteomes; UP000004712; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF2; M18 FAMILY AMINOPEPTIDASE 1-RELATED; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004712};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   465 AA;  51586 MW;  EE77FA34EE3C3118 CRC64;
     MIVLNFEELE LNSKSIWQLV GEEEHREIYA YGDRYKNFLD NAKTEREACK FIIAEAVKNG
     FVSFEEAIKG KIKQGDKIYL NNKNKSAVLF VMGEDLTEGM RIVGSHIDCP RLDIKQRPLY
     EDLEMAFLKT HYYGGIKKYQ WPTIPLALHG YVVNSNGESF DIRIGENEDD PVFYINDLLP
     HLGADQNKKV LGEAIPGESL NIVVGHSSYG IKEDKNPIKK AVLKYLNENY GIVEEDFMVA
     EFEVVPATKA RDVGFDRAMI AAHGHDDRIC SYANLEAILK TENPKITAVG LFVDKEEIGS
     VGNSSMSAKF FENAVAEILA TGENYSDILV RRAMANSKVL SADVTAALDP DFKEVMDSKN
     AAVVGYGIAM SKYTGARGKS GCNDANSEFL VELRDIFKRD NVIWQTGELG KVDQGGGGTI
     AYILAEYGAE VVDMGTAMLS MHAPVELASK ADAYMTFKAY KSFLK
//