ID F9MQX9_9FIRM Unreviewed; 455 AA.
AC F9MQX9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=HMPREF1040_0513 {ECO:0000313|EMBL:EGS32210.1};
OS Megasphaera sp. UPII 135-E.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1000569 {ECO:0000313|EMBL:EGS32210.1, ECO:0000313|Proteomes:UP000004137};
RN [1] {ECO:0000313|EMBL:EGS32210.1, ECO:0000313|Proteomes:UP000004137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII 135-E {ECO:0000313|EMBL:EGS32210.1,
RC ECO:0000313|Proteomes:UP000004137};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUN-2011) 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}.
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:EGS32210.1}.
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DR EMBL; AFUG01000043; EGS32210.1; -; Genomic_DNA.
DR RefSeq; WP_007393234.1; NZ_AFUG01000043.1.
DR AlphaFoldDB; F9MQX9; -.
DR eggNOG; COG1362; Bacteria.
DR OrthoDB; 89722at2; -.
DR Proteomes; UP000004137; 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:UP000004137};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 455 AA; 50606 MW; B427525F6033E17B CRC64;
MKTFDKEHSA WQRFSTEQRQ EVENYATNYR AFLDTARTER LANKEILRQA TKAGFRSIQE
YTSLQPGDKV FWDQKGKAVV LAIIGKQPLE AGLKIVGSHI DCPRLDLKGM PLVEKDNIAY
FKTHYYGGIL KYQWVCMPLA LLGVVYTASG KRIDVSIGDE PQDPVLYITD LLPHLGKDQI
TKPLGEAITG EMLMPIIGIH SDEDTVKPAI LQLLKEKYNI EEEDFTTAEL EIVPAQKSRD
VGLDRSMIMS HGQDDRVCSY ANLAAILHAH STEKTQVALF ADKEEIGSMG NTGVQASYFL
DFISELLALQ GHKEELYLRR LLRQSEVLSA DVCAALDPNF ESAFEKNNAG RFGYGIALCK
YTGSRGKAGS SDANAEFLIK IRNIFNENNV PWQISELGKV DQGGGGTIAY IMANWGCDVV
DCGVAMLSMH APLELVAKVD AYCAYLAYKA FFESL
//
