ID F8VGZ6_SALBC Unreviewed; 503 AA.
AC F8VGZ6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 06-MAR-2013, entry version 13.
DE RecName: Full=Probable cytosol aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase;
DE AltName: Full=Leucyl aminopeptidase;
GN Name=pepA; OrderedLocusNames=SBG_3897;
OS Salmonella bongori (strain ATCC 43975 / DSM 13772 / NCTC 12419).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=218493;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43975 / DSM 13772 / NCTC 12419;
RX PubMed=21876672; DOI=10.1371/journal.ppat.1002191;
RA Fookes M., Schroeder G.N., Langridge G.C., Blondel C.J., Mammina C.,
RA Connor T.R., Seth-Smith H., Vernikos G.S., Robinson K.S., Sanders M.,
RA Petty N.K., Kingsley R.A., Baumler A.J., Nuccio S.P., Contreras I.,
RA Santiviago C.A., Maskell D., Barrow P., Humphrey T., Nastasi A.,
RA Roberts M., Frankel G., Parkhill J., Dougan G., Thomson N.R.;
RT "Salmonella bongori provides insights into the evolution of the
RT Salmonellae.";
RL PLoS Pathog. 7:E1002191-E1002191(2011).
CC -!- FUNCTION: Presumably involved in the processing and regular
CC turnover of intracellular proteins. Catalyzes the removal of
CC unsubstituted N-terminal amino acids from various peptides (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-
CC Yaa-, in which Xaa is preferably Leu, but may be other amino acids
CC including Pro although not Arg or Lys, and Yaa may be Pro. Amino
CC acid amides and methyl esters are also readily hydrolyzed, but
CC rates on arylamides are exceedingly low.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid,
CC preferentially leucine, but not glutamic or aspartic acids.
CC -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
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DR EMBL; FR877557; CCC32939.1; -; Genomic_DNA.
DR RefSeq; YP_004732681.1; NC_015761.1.
DR MEROPS; M17.003; -.
DR GeneID; 10969183; -.
DR KEGG; sbg:SBG_3897; -.
DR KO; K01255; -.
DR BioCyc; SBON218493:GJAH-3946-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:HAMAP.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1; -.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963:SF3; PTHR11963:SF3; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Protease.
FT ACT_SITE 282 282 By similarity.
FT ACT_SITE 356 356 By similarity.
FT METAL 270 270 Manganese 2 (By similarity).
FT METAL 275 275 Manganese 1 (By similarity).
FT METAL 275 275 Manganese 2 (By similarity).
FT METAL 293 293 Manganese 2 (By similarity).
FT METAL 352 352 Manganese 1 (By similarity).
FT METAL 354 354 Manganese 1 (By similarity).
FT METAL 354 354 Manganese 2 (By similarity).
SQ SEQUENCE 503 AA; 54867 MW; 4049C24FDC899C51 CRC64;
MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKPGQTL
LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL NDTGSMEAVC FLTELHVKGR
NNYWKVRQAV ETAKETLYSF DQLKTNKSEP RRPLRKMVFN VPTRRELTSG ERAIQHGLAI
AAGIKAAKDL GNMPPNICNA AYLASQARQL ADSYSTNVIT RVIGEQQMRE LGMNAYLAVG
HGSQNESLMS VIEYKGNSSE EARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV
YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN TDAEGRLVLC
DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMSNHN PLAHELIGAS EQAGDRAWRL
PLGDEYQEQL ESNFADMANI GGRPGGAITA GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG
ATGRPVALLA QFLLNRAGFN GEE
//
