AMPA2_SHEON
ID AMPA2_SHEON Reviewed; 502 AA.
AC Q8EH62;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable cytosol aminopeptidase 2;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase 2;
DE Short=LAP 2;
DE EC=3.4.11.10;
DE AltName: Full=Leucyl aminopeptidase 2;
GN Name=pepA2; Synonyms=pepA-2; OrderedLocusNames=SO_1368;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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}.
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DR EMBL; AE014299; AAN54433.1; -; Genomic_DNA.
DR RefSeq; NP_716988.1; NC_004347.2.
DR RefSeq; WP_011071577.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EH62; -.
DR SMR; Q8EH62; -.
DR STRING; 211586.SO_1368; -.
DR MEROPS; M17.003; -.
DR PaxDb; Q8EH62; -.
DR PRIDE; Q8EH62; -.
DR KEGG; son:SO_1368; -.
DR PATRIC; fig|211586.12.peg.1317; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_2_2_6; -.
DR OMA; MKNTGPR; -.
DR OrthoDB; 356206at2; -.
DR PhylomeDB; Q8EH62; -.
DR BioCyc; SONE211586:G1GMP-1266-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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..502
FT /note="Probable cytosol aminopeptidase 2"
FT /id="PRO_0000165797"
FT ACT_SITE 281
FT /evidence="ECO:0000255"
FT ACT_SITE 355
FT /evidence="ECO:0000255"
FT BINDING 269
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 502 AA; 54723 MW; CD7879C50F0C2FB1 CRC64;
MEFSVKSGSP EKQRSACIVV GVYEPRRLSG IAEQLDKISE GYISNLLRRG DLEGKPGQML
LLHHVPNVLS ERVLLVGCGK ERELDERQYK QIITKTINTL NETGSMEAVC FLTELHVKGR
DTYWKVRQAV ETTNSSLYCF DALKTRKGET RRPLRKLVFN VPTRRELTLG ERAIEHGMAV
SSGMHLCRDV ANMPPNICNP AYLASQARQL AEIHENLHVS TVGEEQMAKL GMNSYLAVGR
ASANESIMTV MEYKGAVDST EKPIVLIGKG LTFDSGGISL KPGEAMDEMK YDMGGAAGVI
GTMKAICEMK LPINVVGILA GCENMPSGNA YRPGDILTTL SGQTVEVLNT DAEGRLVLCD
VLTYVERFDP ELVIDTATLT GACVIALGKH ASGLFSSHNP LAHELLNAGE QSGDRAWRMP
LWDEYQDMLD SPFADMTNLG GRPAGAITAA CFLSRFAKKY NWAHLDVAGT AWNSGANKGS
TGRPVPILTQ FLINRAGVEL GE
