ID   A0A0M2H9Y5_9MICO        Unreviewed;       433 AA.
AC   A0A0M2H9Y5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=apeB {ECO:0000313|EMBL:KJL41459.1};
GN   ORFNames=RS82_02688 {ECO:0000313|EMBL:KJL41459.1};
OS   Microbacterium trichothecenolyticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL41459.1, ECO:0000313|Proteomes:UP000034098};
RN   [1] {ECO:0000313|EMBL:KJL41459.1, ECO:0000313|Proteomes:UP000034098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL41459.1,
RC   ECO:0000313|Proteomes:UP000034098};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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:KJL41459.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JYJA01000037; KJL41459.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2H9Y5; -.
DR   PATRIC; fig|69370.6.peg.2730; -.
DR   Proteomes; UP000034098; 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   Reference proteome {ECO:0000313|Proteomes:UP000034098};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   433 AA;  45164 MW;  F49C728AD556F471 CRC64;
     MPSSIAPARP AALAHADDLA AFVAASPSSF HAAAEVASRL EDAGFTRLDE AAGWPAPAGG
     KYVVVRDGAA IAWVVPKGAS ASTGVRIFGA HSDSPGFKLK PKPTTGKLGW LQAGVEIYGG
     PLLNSWLDRE LRLAGRLVLD DGTAVLAATG PLLRLPQLAI HLDREVNDHL ALDKQSQTQP
     VWGLGEAESA DILGELAREA GVDAARVRGY DVVTADAARG AAFGRDDVFF ASGRLDDLAS
     VHAGVVALER AADGHDADHI AMLAVFDHEE VGSGTRSGAA GPFLSDVLER LWLSLGADRE
     QQLRALAASW CVSSDVGHSV HPNYPDKHDP VVQPVLGSGP ILKINANQRY ATDAAGAAAW
     NGWCAAAGVT SQEFVSNNAV PCGSTIGPIT ATRLGIRTVD VGIPILSMHS ARELAGVSDL
     WDLARVAETY FRA
//