ID E1LCL8_9FIRM Unreviewed; 463 AA.
AC E1LCL8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=HMPREF9684_1805 {ECO:0000313|EMBL:EFL57684.1};
OS Veillonella atypica ACS-134-V-Col7a.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=866778 {ECO:0000313|EMBL:EFL57684.1, ECO:0000313|Proteomes:UP000005942};
RN [1] {ECO:0000313|EMBL:EFL57684.1, ECO:0000313|Proteomes:UP000005942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-134-V-Col7a {ECO:0000313|EMBL:EFL57684.1,
RC ECO:0000313|Proteomes:UP000005942};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (AUG-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}.
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:EFL57684.1}.
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DR EMBL; AEDS01000049; EFL57684.1; -; Genomic_DNA.
DR RefSeq; WP_005380922.1; NZ_AEDS01000049.1.
DR AlphaFoldDB; E1LCL8; -.
DR Proteomes; UP000005942; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 463 AA; 51479 MW; AE0EB49A63EEEF86 CRC64;
MERKYAWHNY DEQTLQDVMS LGDSYRQFLD NGKTERECVI QSVEAAKKAG YVDLKDLIKS
NTPIKAGDKI YYTHMDKSIA LFNIGTDDLD LGMNILGAHI DSPRIDVKQN PQYEDSNLVF
WDTHYYGGIK KYHWVAMPLA IHGVVVKTDG TRININIGDK ESDPVFCITD LLPHLGQEQM
QKNAAKVIEG EALDLLIGSR PVKDEEKEGV TKFINNLLEK EYGFVERDLL SAELEIVPAG
KARDMGFDRS MVLAYGQDDR VCAYTSLVAM LEVDKVKRTT CCLLVDKEEI GSVGATGMQS
RFFENAVAEI LTLMGKPNSV NVRRTLENSR MLSSDVSAGY DPLYASAFEK KNASYLGMGV
VFNKFTGSRG KSGSNDANAE YMGFIRRVME SNNVTYQTAE LGKVDLGGGG TIAYIMALYG
MNVIDCGVAV LSMHAPWEVT SKADIYEAKR CYVAFLNADD ETI
//
