AMPA_HELPY
ID AMPA_HELPY Reviewed; 496 AA.
AC O25294;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=HP_0570;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07638.1; -; Genomic_DNA.
DR PIR; B64591; B64591.
DR RefSeq; NP_207365.1; NC_000915.1.
DR RefSeq; WP_000912892.1; NC_018939.1.
DR PDB; 4ZI6; X-ray; 2.00 A; A/B/C/D/E/F=1-496.
DR PDB; 4ZLA; X-ray; 1.90 A; A/B/C/D/E/F=1-496.
DR PDBsum; 4ZI6; -.
DR PDBsum; 4ZLA; -.
DR AlphaFoldDB; O25294; -.
DR SMR; O25294; -.
DR DIP; DIP-3140N; -.
DR IntAct; O25294; 2.
DR MINT; O25294; -.
DR STRING; 85962.C694_02940; -.
DR MEROPS; M17.016; -.
DR PaxDb; O25294; -.
DR EnsemblBacteria; AAD07638; AAD07638; HP_0570.
DR KEGG; hpy:HP_0570; -.
DR PATRIC; fig|85962.47.peg.615; -.
DR eggNOG; COG0260; Bacteria.
DR OMA; MKNTGPR; -.
DR PhylomeDB; O25294; -.
DR BRENDA; 3.4.11.10; 2604.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; 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 PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 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..496
FT /note="Cytosol aminopeptidase"
FT /id="PRO_0000165760"
FT ACT_SITE 270
FT /evidence="ECO:0000255"
FT ACT_SITE 344
FT /evidence="ECO:0000255"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4ZLA"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:4ZLA"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 156..182
FT /evidence="ECO:0007829|PDB:4ZLA"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 190..204
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:4ZLA"
FT TURN 229..234
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 252..263
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 283..298
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 301..313
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 343..355
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 388..401
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 421..428
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 435..444
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 449..454
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:4ZLA"
FT TURN 461..464
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:4ZLA"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:4ZLA"
FT HELIX 482..494
FT /evidence="ECO:0007829|PDB:4ZLA"
SQ SEQUENCE 496 AA; 54433 MW; 565A0DBCA825FCC7 CRC64;
MLKIKLEKTT FENAKAECSL VFIINKDFSH AWVKNKELLE TFKYEGEGVF LDQENKILYA
GVKEDDVHLL RESACLAVRT LKKLAFKSVK VGVYTCGAHS KDNALLENLK ALFLGLKLGL
YEYDTFKSNK KESVLKEAIV ALELHKPCEK TCANSLEKSA KEALKYAEIM TESLNIVKDL
VNTPPMIGTP VYMAEVAQKV AKENHLEIHV HDEKFLEEKK MNAFLAVNKA SLSVNPPRLI
HLVYKPKKAK KKIALVGKGL TYDCGGLSLK PADYMVTMKA DKGGGSAVIG LLNALAKLGV
EAEVHGIIGA TENMIGPAAY KPDDILISKE GKSIEVRNTD AEGRLVLADC LSYAQDLNPD
VIVDFATLTG ACVVGLGEFT SAIMGHNEEL KNLFETSGLE SGELLAKLPF NRHLKKLIES
KIADVCNISS SRYGGAITAG LFLNEFIRDE FKDKWLHIDI AGPAYVEKEW DVNSFGASGA
GVRACTAFVE ELLKKA
