AMPA_RICPR
ID AMPA_RICPR Reviewed; 500 AA.
AC P27888;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cytosol aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase;
DE Short=LAP;
DE EC=3.4.11.10;
DE AltName: Full=Leucyl aminopeptidase;
GN Name=pepA; OrderedLocusNames=RP142;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=8416891; DOI=10.1128/jb.175.1.159-165.1993;
RA Wood D.O., Solomon M.J., Speed R.R.;
RT "Characterization of the Rickettsia prowazekii pepA gene encoding leucine
RT aminopeptidase.";
RL J. Bacteriol. 175:159-165(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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.
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; M68966; AAA26388.1; -; Genomic_DNA.
DR EMBL; AJ235270; CAA14610.1; -; Genomic_DNA.
DR PIR; A40631; A40631.
DR RefSeq; NP_220533.1; NC_000963.1.
DR RefSeq; WP_004597194.1; NC_000963.1.
DR AlphaFoldDB; P27888; -.
DR SMR; P27888; -.
DR STRING; 272947.RP142; -.
DR EnsemblBacteria; CAA14610; CAA14610; CAA14610.
DR GeneID; 57569270; -.
DR KEGG; rpr:RP142; -.
DR PATRIC; fig|272947.5.peg.145; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_2_2_5; -.
DR OMA; MKNTGPR; -.
DR Proteomes; UP000002480; 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..500
FT /note="Cytosol aminopeptidase"
FT /id="PRO_0000165792"
FT ACT_SITE 277
FT /evidence="ECO:0000255"
FT ACT_SITE 351
FT /evidence="ECO:0000255"
FT BINDING 265
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 500 AA; 54006 MW; E87FFDEA47EC7C83 CRC64;
MLNINFVNEE SSTNQGLIVF IDEQLKLNNN LIALDQQHYE LISKTIQNKL QFSGNYGQIT
VVPSVIKSCA VKYLIIVGLG NVEKLTEAKI EELGGKILQH ATCAKIATIG LKIINRINRF
TSPTFTSLIA SGAFLASYRF HKYKTTLKEV EKFAVESIEI LTDNNSEAMK LFEVKKLIAE
AVFFTRDISN EPSNIKTPQV YAERIVEILE PLGVNIDVIG EHDIKNLGMG ALLGVGQGSQ
NESKLVVMEY KGGSRDDSTL ALVGKGVIFD TGGISLKPSS NMHLMRYDMA GSAAVVGTII
ALASQKVPVN VVGVVGLVEN MQSGNAQRPG DVVVTMSGQT AEVLNTDAEG RLVLADTVWY
VQEKFNPKCV IDVATLTGAI TVALGSTYAG CFSNNDELAD KLIKAGEAVN EKLWRMPLHD
DYDAMINSDI ADIANIGNVP GAAGSCTAAH FIKRFIKDGV DWAHLDIAGV ANSNNASALC
PKGAVGYGVR LLEKFIKEYN
