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
//