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AMPA_VARPS
ID   AMPA_VARPS              Reviewed;         511 AA.
AC   C5CLU5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Vapar_2730;
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S110;
RX   PubMed=21183664; DOI=10.1128/jb.00925-10;
RA   Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA   O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA   Ovchinnikova G., Goodwin L., Han C.;
RT   "Complete genome sequence of the metabolically versatile plant growth-
RT   promoting endophyte, Variovorax paradoxus S110.";
RL   J. Bacteriol. 193:1183-1190(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: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; CP001635; ACS19352.1; -; Genomic_DNA.
DR   RefSeq; WP_012747834.1; NC_012791.1.
DR   AlphaFoldDB; C5CLU5; -.
DR   SMR; C5CLU5; -.
DR   STRING; 543728.Vapar_2730; -.
DR   MEROPS; M17.003; -.
DR   EnsemblBacteria; ACS19352; ACS19352; Vapar_2730.
DR   GeneID; 45056997; -.
DR   KEGG; vap:Vapar_2730; -.
DR   eggNOG; COG0260; Bacteria.
DR   HOGENOM; CLU_013734_0_1_4; -.
DR   OMA; MKNTGPR; -.
DR   OrthoDB; 356206at2; -.
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.
FT   CHAIN           1..511
FT                   /note="Probable cytosol aminopeptidase"
FT                   /id="PRO_1000203843"
FT   REGION          485..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   ACT_SITE        341
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         255
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         260
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         260
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         278
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         337
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         339
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         339
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   511 AA;  52626 MW;  9B178E092FA435C2 CRC64;
     MDFQLKTLTV ARAAAEKSDV LIVLVGSAPL TAKDPLSALI ASARKAGDLP DKAGKLLALY
     HPDEVVASRV VLAAIGDGKP ASVRSGVIAA VNAAKAYGPK RVVMAFAQEA DGAAVGSAVA
     AAADASYVYT TTKAKTSNGE NGRTIRHLTL GVADAAAVGT AFDEARATVA GIELAKEWGN
     RPGNYCTPTL LAEAAKELGK LPRVKCEVLG PKEVQKLGMG SFAAVAQGSA EPLRFIVLRY
     QGGPKDQAPV VLVGKGITFD TGGVSLKPAA EMDEMKFDMC GAASVLGTFR ALGEIQPAIN
     VVGLVPSCEN MNDGRAIKPG DVVTSMSGQT IEVLNTDAEG RLILCDALTY AKRFEPAAVI
     DIATLTGACV VALGGVRSGL FTSDDSLAEA LQAAGEQSQD RCWRLPLDDE YAEGLKSNFA
     DVANVAGRAG GAITAAKFLQ RFAGDFTWAH LDIAGTAWKS GAAKGSTGRP VGLLVSYLME
     RARSGAAQAV SPKKAARKEP GAAARKARSA Q
 
 
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