(data stored in ACNUC7421 zone)

SWISSPROT: AMPA_ALCBS

ID   AMPA_ALCBS              Reviewed;         489 AA.
AC   Q0VSA5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 80.
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=ABO_0495;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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}.
DR   EMBL; AM286690; CAL15943.1; -; Genomic_DNA.
DR   RefSeq; WP_011587781.1; NC_008260.1.
DR   SMR; Q0VSA5; -.
DR   STRING; 393595.ABO_0495; -.
DR   PRIDE; Q0VSA5; -.
DR   EnsemblBacteria; CAL15943; CAL15943; ABO_0495.
DR   KEGG; abo:ABO_0495; -.
DR   eggNOG; ENOG4105BZ6; Bacteria.
DR   eggNOG; COG0260; LUCA.
DR   HOGENOM; HOG000243132; -.
DR   KO; K01255; -.
DR   OMA; MKNTGPR; -.
DR   OrthoDB; 356206at2; -.
DR   BioCyc; ABOR393595:ABO_RS02575-MONOMER; -.
DR   Proteomes; UP000008871; 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; Q0VSA5.
DR   SWISS-2DPAGE; Q0VSA5.
KW   Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease;
KW   Reference proteome.
FT   CHAIN           1..489
FT                   /note="Probable cytosol aminopeptidase"
FT                   /id="PRO_1000071653"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   ACT_SITE        346
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           260
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           265
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           265
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           283
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           342
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           344
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           344
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   489 AA;  52501 MW;  8D157C58349417BF CRC64;
     MDFAVSNRPL EKSKADALVV LLGKKNDLPQ ALPSATREQI SQFTKAGDFN ASKGQLVWLH
     APQDLNADRL LLVGTGDSPL SDQGWLSLVH KATKTLASSP VKQAMWLLDD THTQTLEWQV
     REGSRVVEES TYRFDNYRSK PAPASNLAKL TFWHAEKDTT LTKAHKTGKA VGLGVNVARD
     LGNLPPNDCY PEYLSGVARD LGKEYEKLTV KVLSQAQAEK MGMGAFHAVA KGSERQGQII
     VMEYKGAKPT KQGPVALVGK GITFDTGGIS LKPGATMDEM KYDMGGAASV FGSVKTVCEL
     DLPIHLVAVV AAAENMPDGR AARPGDIVKT LSGQTVEILN TDAEGRLVLC DALTYVQQKH
     KPHTVIDIAT LTGACVVALG AHAQAVYSND DDLSEALLAA GKETGDRGWP MPLWDEYQGQ
     LDSPFADMQN IGGPKAGSIT AACFLSRFTK EVKWAHLDIA GTAWISGGMS KGATGRPVPM
     LTRYLMDNA
//

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