ID   AMPA_SYNE7              Reviewed;         486 AA.
AC   O06865; Q31NZ9; Q8KPQ6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable cytosol aminopeptidase;
DE            EC=3.4.11.1;
DE   AltName: Full=Leucine aminopeptidase;
DE            Short=LAP;
DE            EC=3.4.11.10;
DE   AltName: Full=Leucyl aminopeptidase;
GN   Name=pepA; Synonyms=ampA, lap; OrderedLocusNames=Synpcc7942_1190;
GN   ORFNames=SEE0038;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., McMurtry S.,
RA   Gonzalez A., Salinas I., Golden S.S., Youderian P.;
RT   "Synechococcus elongatus PCC7942 cosmid 7G3.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-486.
RA   Rubio L.M., Flores E., Herrero A.;
RT   "The narC locus of Synechococcus sp. strain PCC 7942 corresponds to a mobA
RT   gene for molybdopterin guanine dinucleotide biosynthesis.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Presumably involved in the processing and regular turnover of
CC       intracellular proteins. Catalyzes the removal of unsubstituted N-
CC       terminal amino acids from various peptides (By similarity).
CC       {ECO:0000250}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, preferentially leucine,
CC         but not glutamic or aspartic acids.; EC=3.4.11.10;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM82713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY120853; AAM82713.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000100; ABB57220.1; -; Genomic_DNA.
DR   EMBL; Y13330; CAA73771.1; -; Genomic_DNA.
DR   RefSeq; WP_011377907.1; NC_007604.1.
DR   AlphaFoldDB; O06865; -.
DR   SMR; O06865; -.
DR   STRING; 1140.Synpcc7942_1190; -.
DR   MEROPS; M17.A01; -.
DR   PRIDE; O06865; -.
DR   EnsemblBacteria; ABB57220; ABB57220; Synpcc7942_1190.
DR   KEGG; syf:Synpcc7942_1190; -.
DR   eggNOG; COG0260; Bacteria.
DR   HOGENOM; CLU_013734_5_1_3; -.
DR   OMA; MKNTGPR; -.
DR   OrthoDB; 356206at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1190-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00433; Peptidase_M17; 1.
DR   Gene3D; 3.40.220.10; -; 1.
DR   HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR   InterPro; IPR008283; Peptidase_M17_N.
DR   PANTHER; PTHR11963; PTHR11963; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF02789; Peptidase_M17_N; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Protease.
FT   CHAIN           1..486
FT                   /note="Probable cytosol aminopeptidase"
FT                   /id="PRO_0000165803"
FT   CONFLICT        364
FT                   /note="L -> R (in Ref. 3; CAA73771)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   486 AA;  51006 MW;  36502365C3E77B0E CRC64;
     MTFQAIATHP QDWTGDTLAL GLTTAAIGET LSSELQKLDQ QWNGVLQELI SDSEFKAKLA
     ETTTTRIGGS IRKLILVGLG ESPTTEDYRR AAAAVAKQAR SFKSQTLAIA FPPSDDPAAI
     ASAIVEGISL ALYKDQRFKS EPDTASGPSS IELLGLAGQE AAIARAEQVV AGVELARQLV
     AAPANVVTPV TMADTAQELA AELGLELEIL EADECEKRGM GAFLGVAKAS DLPPKFIHLT
     YRPESTPRRK LAIVGKGLTF DSGGYNIKGA GSGIEMMKTD MGGAAATLGA AKAIGLIKPD
     VEVHFISAVT ENMISGRGMH PGDILTASNG KTIEVNNTDA EGRLTLADAL VFADGLGVDA
     IVDLATLTGA CIIALGDDIA GLWSPSDDLA EQLLQAGKAA GEKLWRLPLE EPYLDGLKSP
     VADYKNTGPR AGGSITAALF LKQFVKHPVW AHLDVAGPVW SDKEKHYNPA GATGYGVRTL
     VNWVLS