ID A0A1Q9JE73_9FIRM Unreviewed; 464 AA.
AC A0A1Q9JE73;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=BIV20_12555 {ECO:0000313|EMBL:OLR54505.1};
OS Roseburia sp. 499.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1261634 {ECO:0000313|EMBL:OLR54505.1, ECO:0000313|Proteomes:UP000186602};
RN [1] {ECO:0000313|EMBL:OLR54505.1, ECO:0000313|Proteomes:UP000186602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=499 {ECO:0000313|EMBL:OLR54505.1,
RC ECO:0000313|Proteomes:UP000186602};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR54505.1}.
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DR EMBL; MJID01000013; OLR54505.1; -; Genomic_DNA.
DR RefSeq; WP_075721351.1; NZ_MJID01000013.1.
DR AlphaFoldDB; A0A1Q9JE73; -.
DR STRING; 1261634.BIV20_12555; -.
DR OrthoDB; 89722at2; -.
DR Proteomes; UP000186602; 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 CDD; cd05659; M18_API; 1.
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:UP000186602};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 464 AA; 51055 MW; 23A7C2347285E26A CRC64;
MERKNAWEKY PEGKREEVFA FAEGYKKFIS DCKTERECVT ELVAQAKSAG FENLDEIIAS
GKTLKTGDKV YAENMGKMLA LFVIGKQPLE KGMNILGAHI DSPRLDLKQN PLYEDTDMAL
LDTHYYGGVK KYQWVTLPLA LHGVVVKKDG TVINVSIGEK EEDPVFGISD LLVHLAGEQM
EKKAAKVIEG EQLDVLVGSI PFLSEKEEEK TKDAVKANVL NILKEQYNIE EDDFLSAEIE
VVPAGKARDY GFDRSMIMGY GHDDRVCAYP SFVATLEVGT CEKTSVCLLV DKEEIGSVGA
TGMQSKFFSY AVAEILEAMG GYSQIAFNRA MSNSKVLSSD VSAAYDPLYA SVMEKKNAAY
FGKGLVFNKY TGSRGKGGSN DANPEYIAEL RRIMDENNVA FQTSELGKVD QGGGGTIAYI
LANYNMSVID SGVAVLNMHA PWEIISKVDI YEAKRGYAAF LKEA
//
