AMPA_BORPE
ID AMPA_BORPE Reviewed; 499 AA.
AC Q7VW48;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BP2421;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(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; BX640418; CAE42692.1; -; Genomic_DNA.
DR RefSeq; NP_881050.1; NC_002929.2.
DR RefSeq; WP_003821370.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VW48; -.
DR SMR; Q7VW48; -.
DR STRING; 257313.BP2421; -.
DR MEROPS; M17.003; -.
DR GeneID; 45389972; -.
DR KEGG; bpe:BP2421; -.
DR PATRIC; fig|257313.5.peg.2609; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_2_2_4; -.
DR OMA; MKNTGPR; -.
DR Proteomes; UP000002676; 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..499
FT /note="Probable cytosol aminopeptidase"
FT /id="PRO_0000165726"
FT ACT_SITE 283
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT ACT_SITE 357
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 276
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 276
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 355
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 355
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ SEQUENCE 499 AA; 51729 MW; EEBD5807F9BFB5C5 CRC64;
MEFSTQTTAS LHQIKTAALA VGVFADGVLS AAAEVIDRAS HGAVAAVVKS EFRGRTGSTL
VLRSLAGVSA QRVVLVGLGK QAEYNARAHA SAEQAFAAAC VAAQVGEGVS TLAGVAIEGV
PVRARARSAA IAAGAAAYHY DATFGKANRD ARPRLKKIVQ VVDRAASAQA QLGLREGAAI
AHGMELTRTL GNLPGNVCTP AYLGNTAKKL AREFKSLKVE VLERKQVEAL GMGSFLSVAR
GSEEPLRFIV LRHAGKPAKK DKAGPVVLVG KGITFDAGGI SLKPAATMDE MKYDMCGAAS
VLGTFRALAE LELPLDVVGL IAACENLPSG KANKPGDVVT SMSGQTIEIL NTDAEGRLVL
CDALTYAERF KPAAVIDIAT LTGACVVALG NVNSGLFSKD DALADALLAA SRQSLDPAWR
LPLDDAYQDQ LKSNFADIAN IGGPPAGAVT AACFLSRFTK AYPWAHLDIA GTAWRGGKDK
GATGRPVPLL MQYLLDQAG
