AMPA_CHLTR
ID AMPA_CHLTR Reviewed; 499 AA.
AC O84049;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=CT_045;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(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 (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; AE001273; AAC67636.1; -; Genomic_DNA.
DR PIR; C71563; C71563.
DR RefSeq; NP_219548.1; NC_000117.1.
DR RefSeq; WP_009871393.1; NC_000117.1.
DR PDB; 6OME; X-ray; 1.95 A; A=2-499.
DR PDBsum; 6OME; -.
DR AlphaFoldDB; O84049; -.
DR SMR; O84049; -.
DR STRING; 813.O172_00245; -.
DR EnsemblBacteria; AAC67636; AAC67636; CT_045.
DR GeneID; 884033; -.
DR KEGG; ctr:CT_045; -.
DR PATRIC; fig|272561.5.peg.51; -.
DR HOGENOM; CLU_013734_2_2_0; -.
DR InParanoid; O84049; -.
DR OMA; MKNTGPR; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Protease; Reference proteome.
FT CHAIN 1..499
FT /note="Probable cytosol aminopeptidase"
FT /id="PRO_0000165741"
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"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 17..26
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 85..101
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 162..187
FT /evidence="ECO:0007829|PDB:6OME"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 288..303
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 306..318
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 376..382
FT /evidence="ECO:0007829|PDB:6OME"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 394..407
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 418..424
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 440..450
FT /evidence="ECO:0007829|PDB:6OME"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:6OME"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:6OME"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:6OME"
FT HELIX 486..496
FT /evidence="ECO:0007829|PDB:6OME"
SQ SEQUENCE 499 AA; 54210 MW; 04F517A9E7FB8254 CRC64;
MVLLYSQASW DKRSKADALV LPFWMKNSKA QEAAVVDEDY KLVYQNALSN FSGKKGETAF
LFGNDHTKEQ KIVLLGLGKS EEVSGTTVLE AYAQATTVLR KAKCKTVNIL LPTISQLRFS
VEEFLTNLAA GVLSLNYNYP TYHKVDTSLP FLEKVTVMGI VSKVGDKIFR KEESLFEGVY
LTRDLVNTNA DEVTPEKLAA VAKDLAGEFA SLDVKILDRK AILKEKMGLL AAVAKGAAVE
PRFIVLDYQG KPKSKDRTVL IGKGVTFDSG GLDLKPGKAM ITMKEDMAGA ATVLGIFSAL
ASLELPINVT GIIPATENAI GSAAYKMGDV YVGMTGLSVE IGSTDAEGRL ILADAISYAL
KYCNPTRIID FATLTGAMVV SLGESVAGFF ANNDVLARDL AEASSETGEA LWRMPLVEKY
DQALHSDIAD MKNIGSNRAG SITAALFLQR FLEDNPVAWA HLDIAGTAYH EKEELPYPKY
ATGFGVRCLI HYMEKFLSK
