(data stored in SCRATCH zone)

SWISSPROT: D3UW88_XENBS

ID   D3UW88_XENBS            Unreviewed;       502 AA.
AC   D3UW88;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Probable cytosol aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181};
DE            EC=3.4.11.1 {ECO:0000256|HAMAP-Rule:MF_00181};
DE   AltName: Full=Leucine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181};
DE            Short=LAP {ECO:0000256|HAMAP-Rule:MF_00181};
DE            EC=3.4.11.10 {ECO:0000256|HAMAP-Rule:MF_00181};
DE   AltName: Full=Leucyl aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181};
GN   Name=pepA {ECO:0000256|HAMAP-Rule:MF_00181,
GN   ECO:0000313|EMBL:CBJ79597.1};
GN   OrderedLocusNames=XBJ1_0447 {ECO:0000313|EMBL:CBJ79597.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79597.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79597.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79597.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(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.
CC       {ECO:0000256|HAMAP-Rule:MF_00181, ECO:0000256|SAAS:SAAS00727879}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which
CC         Xaa is preferably Leu, but may be other amino acids including
CC         Pro although not Arg or Lys, and Yaa may be Pro. Amino acid
CC         amides and methyl esters are also readily hydrolyzed, but rates
CC         on arylamides are exceedingly low.; EC=3.4.11.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00181,
CC         ECO:0000256|SAAS:SAAS01118307};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, preferentially
CC         leucine, but not glutamic or aspartic acids.; EC=3.4.11.10;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00181};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00181};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00181};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181,
CC       ECO:0000256|SAAS:SAAS00759153}.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00181, ECO:0000256|SAAS:SAAS00754360}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FN667741; CBJ79597.1; -; Genomic_DNA.
DR   RefSeq; WP_012987053.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0447; -.
DR   EnsemblBacteria; CBJ79597; CBJ79597; XBJ1_0447.
DR   GeneID; 8830070; -.
DR   KEGG; xbo:XBJ1_0447; -.
DR   PATRIC; fig|406818.4.peg.412; -.
DR   eggNOG; ENOG4105BZ6; Bacteria.
DR   eggNOG; COG0260; LUCA.
DR   HOGENOM; HOG000243132; -.
DR   KO; K01255; -.
DR   OMA; MKNTGPR; -.
DR   BioCyc; XBOV406818:XBJ1_RS01955-MONOMER; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00433; Peptidase_M17; 1.
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; PTHR11963; 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;
DR   PRODOM; D3UW88.
DR   SWISS-2DPAGE; D3UW88.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00754331, ECO:0000313|EMBL:CBJ79597.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00759165};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00754382, ECO:0000313|EMBL:CBJ79597.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00727876};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00754372};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00754389};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN      349    356       CYTOSOL_AP. {ECO:0000259|PROSITE:
FT                                PS00631}.
FT   ACT_SITE    281    281       {ECO:0000256|HAMAP-Rule:MF_00181}.
FT   ACT_SITE    355    355       {ECO:0000256|HAMAP-Rule:MF_00181}.
FT   METAL       269    269       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       274    274       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       274    274       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       292    292       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       351    351       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       353    353       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       353    353       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
SQ   SEQUENCE   502 AA;  54613 MW;  9F57451B704A2F93 CRC64;
     MEFSVKSGSP EKQRSACIIV GVFEPRRLSP IAEQLDKISN GYISALLRRG ELEGKVGQSL
     LLHHVPNVLS ERILLVGCGK ERELDERQYK QIIQKTISTL NETGSMEAVC FLTELHVKGR
     NNYWKVRQAV ETAKESLYVF DQLKSSKNEL RRPLRKIVFN VPTRRELTSG ERAIQHGLAI
     ASGIKASKDL ANMPPNICNA AYLASQARQL ADTADNLNTK VIGEEQMKEL GMNSYLAVGQ
     GSQNESLMSV IEYKGSKDAN AKPIVLVGKG LTFDAGGISL KPGEGMDEMK YDMCGAASVY
     GVMRVIAELQ LPLNVIGVLA GCENMPGGRA FRPGDILTTM SGQTVEVLNT DAEGRLVLCD
     VLTYVERFDP ELVIDVATLT GACVIALGSH YTGLMSNHNP LAHELLNASE QAGDRAWRLP
     MADEYFEQLD SNFADMANIG GRAGGTITAG CFLSRFTTKY NWAHLDIAGT AWRSGKAKGA
     TGRPVALLAQ FLLNRAGLNA DD
//

If you have problems or comments...

PBIL Back to PBIL home page