ID   A0AAE4ZK69_RHOHA        Unreviewed;       433 AA.
AC   A0AAE4ZK69;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   02-OCT-2024, entry version 3.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   ORFNames=GS505_19305 {ECO:0000313|EMBL:NKS27921.1};
OS   Rhodococcus hoagii (Corynebacterium equii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Prescottella.
OX   NCBI_TaxID=43767 {ECO:0000313|EMBL:NKS27921.1, ECO:0000313|Proteomes:UP000605618};
RN   [1] {ECO:0000313|EMBL:NKS27921.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Lh_141_1 {ECO:0000313|EMBL:NKS27921.1};
RX   PubMed=32291839;
RA   Huber L., Giguere S., Slovis N.M., Alvarez-Narvaez S., Hart K.A.,
RA   Greiter M., Morris E.R.A., Cohen N.D.;
RT   "The novel and transferable erm(51) gene confers Macrolides, Lincosamides,
RT   and Streptogramins B (MLSB) resistance to clonal Rhodococcus equi in the
RT   environment.";
RL   Environ. Microbiol. 0:0-0(2020).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|HAMAP-Rule:MF_00467,
CC       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:NKS27921.1}.
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DR   EMBL; WUYZ01000007; NKS27921.1; -; Genomic_DNA.
DR   Proteomes; UP000605618; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
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, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00467};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00467};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}.
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT   BINDING         407
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
SQ   SEQUENCE   433 AA;  45744 MW;  E7F6DE96F7325657 CRC64;
     MMVGMPSMTQ ADAQGLCSFV DASPSPFHVC ATVASELSAN GFTELQETDA WPSAPGRYYL
     VRGGSLIAWS TEGVSAGPAS PFRIVGGHTD SPNLRVKQHP DLVSAGWQLV GLEPYGGAWL
     NSWLDRDLGI SGRLSVRAGD AVQEVLVRVD RPILRVPQLA IHLSEERKGV QLDPQRHLNA
     VWGTGSEPRS FIGFLADEAG VAAEAVLGWE LMTHDLAPST VVGEDASLVS APRLDNQGTC
     YAGTQALLAA VAEPGDSTPV LALFDHEEVG SMSDRGAFSD LLNSVLERIV LLRGGGREDF
     LRAMSGSVCA SGDMAHATHP NYPDRHEPAH RIAINGGPVL KVNQNLRYAS DAAGAAEFAL
     ACDRAGVPLQ RYVHRADLPC GSTIGPITAS RTGLSTVDVG APQLAMHSAR ELMGARDVGM
     YADALAAFLT PVR
//