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AMPA_WOLSU
ID   AMPA_WOLSU              Reviewed;         483 AA.
AC   Q7M8W6;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Probable cytosol aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE            EC=3.4.11.1 {ECO:0000255|HAMAP-Rule:MF_00181};
DE   AltName: Full=Leucine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE            Short=LAP {ECO:0000255|HAMAP-Rule:MF_00181};
DE            EC=3.4.11.10 {ECO:0000255|HAMAP-Rule:MF_00181};
DE   AltName: Full=Leucyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
GN   Name=pepA {ECO:0000255|HAMAP-Rule:MF_00181}; OrderedLocusNames=WS1353;
OS   Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS   11488 / FDC 602W) (Vibrio succinogenes).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Wolinella.
OX   NCBI_TaxID=273121;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC   11488 / FDC 602W;
RX   PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA   Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA   Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA   Meyer F., Lederer H., Schuster S.C.;
RT   "Complete genome sequence and analysis of Wolinella succinogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00181}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00181};
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00181};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00181}.
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DR   EMBL; BX571660; CAE10424.1; -; Genomic_DNA.
DR   RefSeq; WP_011139210.1; NC_005090.1.
DR   AlphaFoldDB; Q7M8W6; -.
DR   SMR; Q7M8W6; -.
DR   STRING; 273121.WS1353; -.
DR   MEROPS; M17.016; -.
DR   EnsemblBacteria; CAE10424; CAE10424; WS1353.
DR   KEGG; wsu:WS1353; -.
DR   eggNOG; COG0260; Bacteria.
DR   HOGENOM; CLU_013734_2_2_7; -.
DR   OMA; MKNTGPR; -.
DR   OrthoDB; 356206at2; -.
DR   Proteomes; UP000000422; Chromosome.
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; Metal-binding; Protease;
KW   Reference proteome.
FT   CHAIN           1..483
FT                   /note="Probable cytosol aminopeptidase"
FT                   /id="PRO_0000165815"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         250
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         250
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         268
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         327
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         329
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         329
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   483 AA;  53076 MW;  D4C5DF1F17DDC8B3 CRC64;
     MEILCHSAPL HEIKAEASLI FVINKEFSHE WIADSELFGS VGFEGKEGQT LFIPQSKTLY
     YALDSLTPDS IRESSAKALR ALKKYPFSSF KVGIYTQESL ECLEAMAAGF LLGDYNFETY
     KSQKSESKLT QILISLQTHL GRQIDSKSFE TILARQSAIA RAVNLARELV NTPPEDATPQ
     KIAQAAQKVA QEHQLECRIE DEKFLEKEQM GAFLAVSRAS IHRPRLIHLT HQSPKPKLKV
     ALVGKGLTYD SGGLSLKPAD FMVTMKADKG GGCAVIAILQ AAKELGLELE LHGIVGATEN
     MIGGNAYKPD DVLRAKNGKT IEIRNTDAEG RLVLADCLVY AQELKPDYII DLATLTGACV
     VGLGEYTSGV LGHSQELKHR FIECATQSGE LTADLPFNRH LKKLIESKVA DVCNVSSTRY
     GGSITAGLFL SEFIEESYKE KWLHLDIAGP AYVEKEWDVN PHGASGAGVR MVLQFLEQLT
     KES
 
 
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