ID B2URM0_AKKM8 Unreviewed; 369 AA.
AC B2URM0;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:ACD05105.1};
GN OrderedLocusNames=Amuc_1280 {ECO:0000313|EMBL:ACD05105.1};
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD05105.1, ECO:0000313|Proteomes:UP000001031};
RN [1] {ECO:0000313|Proteomes:UP000001031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M29 family.
CC {ECO:0000256|ARBA:ARBA00008236}.
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DR EMBL; CP001071; ACD05105.1; -; Genomic_DNA.
DR RefSeq; WP_012420320.1; NZ_CP071807.1.
DR AlphaFoldDB; B2URM0; -.
DR STRING; 349741.Amuc_1280; -.
DR PaxDb; 349741-Amuc_1280; -.
DR KEGG; amu:Amuc_1280; -.
DR eggNOG; COG2309; Bacteria.
DR HOGENOM; CLU_057697_0_0_0; -.
DR OrthoDB; 9803993at2; -.
DR BioCyc; AMUC349741:G1GBX-1368-MONOMER; -.
DR Proteomes; UP000001031; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR34448:SF1; BLL6088 PROTEIN; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR PRINTS; PR00919; THERMOPTASE.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:ACD05105.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001031}.
SQ SEQUENCE 369 AA; 40485 MW; F4C05E4DAF354818 CRC64;
MRDPRFQALA AQLAGYSTAL RPGDRVLLEL TDIPEEMGIA LIREARNAGA IPFLRLNQSR
LNREMLSGAT EEQYGIIGRH RLAEMEDMDA YIEIRGGGNA FELSSVPQEN MAAAMKALNP
VSQRRIRHTR WCGLRWPSGG MAQQAAMSTE EFEDFYFRTC LMDYAALRPA MRKLAAMMEK
AEYVKITGPG TDISFSIKGL PAIPCAGECN LPDGEVFTAP VIDSANGHIS FNTPSLFQGI
PFDNIRLTLK NGLVVHAEAG DKTGELNAIL DTDPGARRLG EFAFGVNPAI TRPMRNILFD
EKISGSFHLT PGQAYHVADN GNQSRIHWDM VCIQTEAAGG GDIYLDGKLV RRNGLFTLPE
LAILNPSLS
//
