AMPA_CHLPN
ID AMPA_CHLPN Reviewed; 499 AA.
AC Q9Z8F8; Q9JQJ2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable 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=CPn_0385, CP_0370, CpB0397;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; AE001363; AAD18529.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38219.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98593.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98328.1; -; Genomic_DNA.
DR PIR; G72083; G72083.
DR PIR; G86538; G86538.
DR RefSeq; NP_224585.1; NC_000922.1.
DR RefSeq; WP_010883028.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z8F8; -.
DR SMR; Q9Z8F8; -.
DR STRING; 115711.CP_0370; -.
DR PRIDE; Q9Z8F8; -.
DR EnsemblBacteria; AAD18529; AAD18529; CPn_0385.
DR EnsemblBacteria; AAF38219; AAF38219; CP_0370.
DR GeneID; 45050432; -.
DR KEGG; cpa:CP_0370; -.
DR KEGG; cpj:pepA; -.
DR KEGG; cpn:CPn_0385; -.
DR KEGG; cpt:CpB0397; -.
DR PATRIC; fig|115713.3.peg.427; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_2_2_0; -.
DR OrthoDB; 356206at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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.
FT CHAIN 1..499
FT /note="Probable cytosol aminopeptidase"
FT /id="PRO_0000165739"
FT ACT_SITE 275
FT /evidence="ECO:0000255"
FT ACT_SITE 349
FT /evidence="ECO:0000255"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
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 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 499 AA; 54510 MW; B0F281B1DF4B9EC2 CRC64;
MVLFHAQASG RNRVKADAIV LPFWHFKDAK NAASFEAEFE PSYLPALENF QGKTGEIELL
YSSPKAKEKR IVLLGLGKNE ELTSDVVFQT YATLTRVLRK AKCSTVNIIL PTISELRLSA
EEFLVGLSSG ILSLNYDYPR YNKVDRNLET PLSKVTVIGI VPKMADAIFR KEAAIFEGVY
LTRDLVNRNA DEITPKKLAE VALNLGKEFP SIDTKVLGKD AIAKEKMGLL LAVSKGSCVD
PHFIVVRYQG RPKSKDHTVL IGKGVTFDSG GLDLKPGKSM LTMKEDMAGG ATVLGILSAL
AVLELPINVT GIIPATENAI DGASYKMGDV YVGMSGLSVE ICSTDAEGRL ILADAITYAL
KYCKPTRIID FATLTGAMVV SLGEEVAGFF SNNDVLAEDL LEASAETSEP LWRLPLVKKY
DKTLHSDIAD MKNLGSNRAG AITAALFLQR FLEESSVAWA HLDIAGTAYH EKEEDRYPKY
ASGFGVRSIL YYLENSLSK
