(data stored in SCRATCH3701 zone)

SWISSPROT: AMPA_RICTY

ID   AMPA_RICTY              Reviewed;         500 AA.
AC   Q68XM6;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 85.
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=RT0131;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03616.1; -; Genomic_DNA.
DR   RefSeq; WP_011190603.1; NC_006142.1.
DR   SMR; Q68XM6; -.
DR   STRING; 257363.RT0131; -.
DR   MEROPS; M17.003; -.
DR   PRIDE; Q68XM6; -.
DR   EnsemblBacteria; AAU03616; AAU03616; RT0131.
DR   KEGG; rty:RT0131; -.
DR   eggNOG; ENOG4105BZ6; Bacteria.
DR   eggNOG; COG0260; LUCA.
DR   HOGENOM; HOG000243129; -.
DR   KO; K01255; -.
DR   OMA; MKNTGPR; -.
DR   OrthoDB; 356206at2; -.
DR   BioCyc; RTYP257363:G1G0L-137-MONOMER; -.
DR   Proteomes; UP000000604; 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; Q68XM6.
DR   SWISS-2DPAGE; Q68XM6.
KW   Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease.
FT   CHAIN           1..500
FT                   /note="Probable cytosol aminopeptidase"
FT                   /id="PRO_0000165793"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   ACT_SITE        351
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           270
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           270
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           288
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           347
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           349
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           349
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   500 AA;  54027 MW;  CF1C5AA45976B488 CRC64;
     MLNINFVNEE SSTNQGLIVF IDEQLKFDTS LMALDQQHYG LISKTIQNKL QFRGNYGQIT
     IVPSVIKSGE VKYLIIVGLG NAEKLTEAKI EELGGKILQH ATCAKISTIG LKIMSRINRF
     TPQTFTSLIA SGAFLASYRF HKYKTTLKEV EKFAVESIEI FTDNNSEAIK LFEVKKLIAE
     AVFFTRDISN EPSNIKTPQV YAERIVDILE PLGVNVDVIG ERDIKNLGMG ALLGVGQGSQ
     NESKLVVMEY KGGSRDDSTI ALVGKGVIFD TGGISLKPSS NMHLMRYDMA GSAAVVGAII
     ALASQKATVN VVGVVGLVEN MQSGNAQRPG DVVVTMSGQT AEVLNTDAEG RLVLADTVWY
     VQEKFNPKCV IDVATLTGAI TVALGSTYAG CFSNNDELAD KLIKAGEEVN EKLWRMPLHD
     DYDAMINSDI ADIANIGNVP GAAGSCTAAH FIKRFIKDGV DWAHLDIAGV ANSNNASALG
     PKGAVGYGVR LLEKFIKEYN
//

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