ID   APE2_SACS2              Reviewed;         785 AA.
AC   P95928;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Leucyl aminopeptidase;
DE            EC=3.4.11.1;
GN   Name=ape2; Synonyms=lap; OrderedLocusNames=SSO2154; ORFNames=C01_030;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-7.
RC   STRAIN=DSM 5833 / MT-4;
RX   PubMed=9723917; DOI=10.1046/j.1365-2958.1998.00971.x;
RA   Condo I., Ruggero D., Reinhardt R., Londei P.;
RT   "A novel aminopeptidase associated with the 60 kDa chaperonin in the
RT   thermophilic archaeon Sulfolobus solfataricus.";
RL   Mol. Microbiol. 29:775-785(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA   Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA   Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA   Ragan M.A., Charlebois R.L.;
RT   "Organizational characteristics and information content of an archaeal
RT   genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL   Mol. Microbiol. 22:175-191(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: Preferentially acts as a leucyl-aminopeptidase, although it
CC       also has activity against other substrates.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC         is preferably Leu, but may be other amino acids including Pro
CC         although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC         methyl esters are also readily hydrolyzed, but rates on arylamides
CC         are exceedingly low.; EC=3.4.11.1;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.;
CC       Temperature dependence:
CC         Optimum temperature is 80 degrees Celsius.;
CC   -!- SUBUNIT: Co-immunoprecipitates with the 60 kDa chaperonin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Can be phosphorylated by cell extracts.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; AF043465; AAC63218.1; -; Genomic_DNA.
DR   EMBL; Y08256; CAA69432.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK42330.1; -; Genomic_DNA.
DR   PIR; S73098; S73098.
DR   RefSeq; WP_009992163.1; NC_002754.1.
DR   AlphaFoldDB; P95928; -.
DR   SMR; P95928; -.
DR   STRING; 273057.SSO2154; -.
DR   MEROPS; M01.021; -.
DR   EnsemblBacteria; AAK42330; AAK42330; SSO2154.
DR   GeneID; 44130865; -.
DR   GeneID; 58783393; -.
DR   KEGG; sso:SSO2154; -.
DR   PATRIC; fig|273057.12.peg.2247; -.
DR   eggNOG; arCOG02969; Archaea.
DR   HOGENOM; CLU_003705_0_3_2; -.
DR   InParanoid; P95928; -.
DR   OMA; FIPCVDH; -.
DR   PhylomeDB; P95928; -.
DR   BRENDA; 3.4.11.B3; 6163.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 1.10.390.10; -; 1.
DR   Gene3D; 2.60.40.1730; -; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; SSF63737; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..785
FT                   /note="Leucyl aminopeptidase"
FT                   /id="PRO_0000095107"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         238..242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         277
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            359
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   785 AA;  90515 MW;  73ACFDEB1F2832BD CRC64;
     MIKVNRYEIF LDFSFQTGDY KGYEKIEMES DEETVVLDAV GLKIVKAKVN GKEIEFSQDE
     SRVNVKSGSF SGILEVEFEG KVTERKLVGI YKASYKDGYV ISTQFEATHA RDFIPCFDHP
     AMKARFKLTV RVDKGLKVIS NMPVVREKEE NGKVVYEFDE TPKMSTYLLY LGIGNFEEIR
     DEGKIPTIIV ATIPGKVQKG RFSMQISRNS IEFYEKYFEI PYQLPKVHLI AIPEFAYGAM
     ENWGAITFRE TALLADDSSS VYQKFRVAEV VAHELAHQWF GNLVTLKWWD DLWLNESFAT
     FMSHKAISQL FPSWNFWDYF VLNQTSRALE KDSVSTTHPI EAHVRDPNEV EQMFDDISYG
     KGASILRMIE AYVGEENFRR GVVNYLKKFS YSNAQGSDLW NSISEVYGSD ISPIMADWIT
     KPGYPMVRVS VSGKRVSLEQ ERFSLIGNVE NLLYKIPLTM EVNGKVVTHL LDKERDTMVF
     EEDVKSLKVN VNRTGFYRVF YYNNSDLVFN SNLSELDKWG IINDYWAFLL AGKIGFKEYE
     RVISKFFNDK DFLPVNELSN ELFTLHAINP DKYQGIAKEF HRIQLKNWRN SKDELGRLTY
     SNILYRLAAI DDEFSLGLSE LFRFYGSLDS DTRQGVAVAY AITYEDNSVD ELLERFRKET
     FDEEKLRYLT AMLFFRKPYL VGNTLSLILS GEIKKQDIPL TLSTAAYNPY AKSAVLNWIK
     MHINFMREAY KGTGILGRRL AEVIPLIGIG AERETEQFFS NLNMPEAERG IGTGLELLKA
     YSRLK