ID E4UCV7_LIBSC Unreviewed; 500 AA.
AC E4UCV7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 OrderedLocusNames=CKC_02230 {ECO:0000313|EMBL:ADR52197.1};
OS Liberibacter solanacearum (strain CLso-ZC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=658172 {ECO:0000313|EMBL:ADR52197.1, ECO:0000313|Proteomes:UP000007038};
RN [1] {ECO:0000313|Proteomes:UP000007038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLso-ZC1 {ECO:0000313|Proteomes:UP000007038};
RA Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L.,
RA Glynn J.;
RT "Complete genome sequence of Candidatus Liberibacter solanacearum CLso-
RT ZC1.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CLso-ZC1;
RA Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L.,
RA Glynn J.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADR52197.1, ECO:0000313|Proteomes:UP000007038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLso-ZC1 {ECO:0000313|EMBL:ADR52197.1,
RC ECO:0000313|Proteomes:UP000007038};
RX PubMed=21552483; DOI=10.1371/journal.pone.0019135;
RA Lin H., Lou B., Glynn J.M., Doddapaneni H., Civerolo E.L., Chen C.,
RA Duan Y., Zhou L., Vahling C.M.;
RT "The Complete Genome Sequence of 'Candidatus Liberibacter solanacearum',
RT the Bacterium Associated with Potato Zebra Chip Disease.";
RL PLoS ONE 6:E19135-E19135(2011).
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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000135, ECO:0000256|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:0000256|ARBA:ARBA00000967, ECO:0000256|HAMAP-
CC Rule:MF_00181};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-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 -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528, ECO:0000256|HAMAP-Rule:MF_00181}.
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DR EMBL; CP002371; ADR52197.1; -; Genomic_DNA.
DR RefSeq; WP_013461853.1; NC_014774.1.
DR AlphaFoldDB; E4UCV7; -.
DR STRING; 658172.CKC_02230; -.
DR KEGG; lso:CKC_02230; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_6_0_5; -.
DR Proteomes; UP000007038; 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; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 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; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW Rule:MF_00181}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00181};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_00181};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00181};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00181}.
FT DOMAIN 346..353
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT ACT_SITE 278
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT ACT_SITE 352
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 289
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
SQ SEQUENCE 500 AA; 54422 MW; 40F1162B8674D312 CRC64;
MDIKFSFARN PFIKKGGMAI LLKTNFSDVT GLSFVGSLGV VERAASVKNF TGESKSHLNI
LVPEGCVWDR LVVVGIGDPR IKDEKFSWLK AGGNAASFIE EDKNIEIFVD VPEYPITKEE
IRDFTLGFIL KLYNFDRYKT KKKEDSSLQS NDSINDSISV TFITQTFEQS NPVVADIKSV
VNGVNLARDI VNEPANVLGT DEFCEQVKKL ESLGVEVDIL DKDTMAQLGM NALLAVSQGS
SRPPYLVVMK WNGGNQCDQP LAFIGKGVVF DSGGISLKPS NGMEEMKGDL AGAAAVTGLL
SVLAERKAKV NAIGILALVE NMPDSSAQRP GDIVRSLSGQ SIEVINTDAE GRLILADALW
YCHTHYKPAL MIDLATLTGA MVVALGNVYA GLFANNNPLA EQLLSAGLST EELLWRMPMN
DEYNKLIESK FADMKNIGGR GAGSIVAAQF LEKFVKDTSW AHIDIAGTAT GNHPKEINQS
WASGFGVRLL DTFVRDFYEK
//
