ID C4FRB7_9FIRM Unreviewed; 448 AA.
AC C4FRB7;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=VEIDISOL_01340 {ECO:0000313|EMBL:EEP65460.1};
OS Veillonella dispar ATCC 17748.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=546273 {ECO:0000313|EMBL:EEP65460.1, ECO:0000313|Proteomes:UP000003529};
RN [1] {ECO:0000313|EMBL:EEP65460.1, ECO:0000313|Proteomes:UP000003529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17748 {ECO:0000313|EMBL:EEP65460.1,
RC ECO:0000313|Proteomes:UP000003529};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) 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:EEP65460.1}.
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DR EMBL; ACIK02000010; EEP65460.1; -; Genomic_DNA.
DR RefSeq; WP_005386903.1; NZ_GG667604.1.
DR AlphaFoldDB; C4FRB7; -.
DR GeneID; 78367408; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_9; -.
DR OrthoDB; 9764268at2; -.
DR Proteomes; UP000003529; 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:SF3; ASPARTYL AMINOPEPTIDASE; 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 448 AA; 49349 MW; 0B56BD2DE0F2B489 CRC64;
MKFDNEQLLK YIGACTSPYH TVDTSLQMLL DSGFTELNLD DEWQLDSGSY VVNVFGTTLF
AFHIGKKPED TLRIASAHTD FPAIRVKPNP ITSVKGYTKL NVEMYGGLIE NTWLDRPLGA
AGTVVLKGDN AFDVDSVLVD TKRPIAIVPN LAIHMNRTVN DGVKLNRQKE MLPILMMDRK
DKEQSTKSLH DSNNPSLFPE SDTQYDEWTM FLADEVNCDP SEILSYEMTL YPTEQGCVLG
TEGDFISAPR LDNLTSCFGV LSGIIQARKH NANGVRCAIL FDNEEVGSRT KQGGAGMLLP
NLIKRVYDAL GYSNQEMESF ISKGFMISSD VAHGLHPNYP EKNDITNIPT LNKGVALKIA
CSQSYAGDAR AIAIVKGLCD EAEANYQIYV NRSDIPGGST VGSISSAMLP MRTMDVGLPL
LAMHSARELM GANDQEQLNR LMNHFLGD
//
