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Database: UniProt
Entry: A0A1L2ZPS4_9MICC
LinkDB: A0A1L2ZPS4_9MICC
Original site: A0A1L2ZPS4_9MICC 
ID   A0A1L2ZPS4_9MICC        Unreviewed;       430 AA.
AC   A0A1L2ZPS4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=BHE16_08375 {ECO:0000313|EMBL:APF41011.1};
OS   Neomicrococcus aestuarii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Neomicrococcus.
OX   NCBI_TaxID=556325 {ECO:0000313|EMBL:APF41011.1, ECO:0000313|Proteomes:UP000183530};
RN   [1] {ECO:0000313|EMBL:APF41011.1, ECO:0000313|Proteomes:UP000183530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B18 {ECO:0000313|EMBL:APF41011.1,
RC   ECO:0000313|Proteomes:UP000183530};
RA   Luo Y.;
RT   "Genome sequencing of Zhihengliuella aestuarii B18 antagonistic to
RT   Plasmodiophora brassicae.";
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; CP018135; APF41011.1; -; Genomic_DNA.
DR   RefSeq; WP_071894488.1; NZ_CP018135.1.
DR   AlphaFoldDB; A0A1L2ZPS4; -.
DR   STRING; 556325.BHE16_08375; -.
DR   KEGG; nae:BHE16_08375; -.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000183530; Chromosome.
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; cd05658; M18_DAP; 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: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:UP000183530};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   430 AA;  45891 MW;  8E12DA58C29B116C CRC64;
     MERTPQFSPA QQHALDLADF VSASPSSFHA VAEGVLRLVA DGFSPLVETE AWNLTPGKYF
     VQRDGALIAF VIPDSATATT GFRILGSHTD SPSFKLKPKP TTSAFGWLQA GVEVYGGPLL
     NSWLDRELVL AGRLVTHDGT EVLTRTAPLL RFPQLAIHLD RGVNEGLKLD PQRHMNPIWG
     TGRAEESDIL AVLADAAGID PLSIGGYDVV ACDAQAPALF GATNEFLASG RLDNLSSVHA
     SLTALLEIAD APGDRIAMIA AFDHEEIGSA SRSGAAGPFL EEVVRRIGFA LGGSLEESYR
     AVADSVCLSS DAGHAIHPNY PERHDPHNQP VAGQGPLLKI NANQRYSTDA LGAAAWTQWC
     ATADARYQEF VSNNAMPCGS TIGPITATRI GIRTLDVGVP LLSMHSAREM AHVEDLYSLS
     RIAHAFFTHS
//
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