ID T0P9F3_9CLOT Unreviewed; 468 AA.
AC T0P9F3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=M918_13725 {ECO:0000313|EMBL:EQB86548.1};
OS Clostridium sp. BL8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB86548.1, ECO:0000313|Proteomes:UP000015873};
RN [1] {ECO:0000313|EMBL:EQB86548.1, ECO:0000313|Proteomes:UP000015873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL8 {ECO:0000313|EMBL:EQB86548.1,
RC ECO:0000313|Proteomes:UP000015873};
RX PubMed=25076986; DOI=10.1186/1757-4749-6-30;
RA Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R.,
RA Shouche Y.S.;
RT "Genome sequencing of multidrug resistant novel Clostridium sp. BL8 reveals
RT its potential for pathogenicity.";
RL Gut Pathog. 6:30-30(2014).
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:EQB86548.1}.
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DR EMBL; AUPA01000220; EQB86548.1; -; Genomic_DNA.
DR RefSeq; WP_021284982.1; NZ_AUPA01000220.1.
DR AlphaFoldDB; T0P9F3; -.
DR STRING; 1354301.M918_13725; -.
DR PATRIC; fig|1354301.3.peg.3864; -.
DR OrthoDB; 89722at2; -.
DR Proteomes; UP000015873; 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:UP000015873};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 468 AA; 51959 MW; FBDE282517A3A214 CRC64;
MGDYNKLVKK YELAWDKYTK EDLDKVFALS ERYIDFMSKC KTERECVNEF IVLAEKEGYR
DINSYIAEGK KLQAGDKVYA NCMGKTLALF LIGSEPVEKG FKILGAHVDS PRLDLKQNPL
YEDSDFAMLK THYYGGVKKY QWVTIPLAIH GVVIKKDGTT VNVVIGEDEK EPVVGISDLL
IHLAGDQMAK TLAKGIEGES LNVCLGSMPI EDKEAKNRVK LNALRLLNEK YGIDEEDFVS
AELEVVPAGR ARSYGLDSSM VMAYGHDDRI CAYTSFEAML NIKETDKTII TLLVDKEEVG
SIGATGMQSR FFENTVAEIV NLMGDYSDLK VRRALANSKM LSSDVSAAFD PNYPSVSEKQ
NNAFFGKGIV FNKYTGARGK GGCNDANPEF IAELRRIMEK HNVSWQTSEL GKVDQGGGGT
IAYILAEYGM EVIDSGVALH NMHAPWEIAS KADIYEACRG YEAFLIEA
//
